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Articles

TOR complex 2 is a master regulator of plasma membrane homeostasis

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Awards

Jeremy Thorner

Biochem J (2022) 479 (18): 1917–1940.

DOI: https://doi.org/10.1042/BCJ20220388

Published: 23 September 2022

...-regulation of the phosphorylation and thus the activity of its essential downstream effector the AGC family protein kinase Ypk1. Through the ensuing effect on the efficiency with which Ypk1 phosphorylates multiple substrates that control diverse processes, membrane homeostasis is maintained. Thus, the major...

View article titled, TOR complex 2 is a master regulator of plasma membrane homeostasis

Includes: Supplementary data

Articles

Divergent kinase WNG1 is regulated by phosphorylation of an atypical activation sub-domain

Pravin S. Dewangan, Tsebaot G. Beraki, E. Ariana Paiz, Delia Appiah Mensah, Zhe Chen, Michael L. Reese

Biochem J (2022) 479 (17): 1877–1889.

DOI: https://doi.org/10.1042/BCJ20220076

Published: 16 September 2022

... into the membrane after trafficking through the parasite secretory system as soluble, chaperoned complexes. A regulator of this process is an atypical protein kinase called WNG1. Phosphorylation by WNG1 appears to serve as a switch for membrane integration. However, like its substrates, WNG1 is secreted from...

View article titled, Divergent kinase WNG1 is regulated by phosphorylation of an atypical activation sub-domain

Includes: Supplementary data

Articles

RIP1 post-translational modifications

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Cell death and survival

Eugene Varfolomeev, Domagoj Vucic

Biochem J (2022) 479 (9): 929–951.

DOI: https://doi.org/10.1042/BCJ20210725

Published: 06 May 2022

... by caspase-8, RIP1 autophosphorylation, and phosphorylation by a number of signaling kinases can greatly impact cellular fate. Disruption of the tightly regulated RIP1 modifications can lead to signaling disbalance in TNF and/or TLR controlled and other inflammatory pathways, and result in severe human...

View article titled, RIP1 post-translational modifications

Articles

Distinct phosphorylation signals drive acceptor versus free ubiquitin chain targeting by parkin

Karen M. Dunkerley, Anne C. Rintala-Dempsey, Giulia Salzano, Roya Tadayon, Dania Hadi, Kathryn R. Barber, Helen Walden, Gary S. Shaw

Biochem J (2022) 479 (6): 751–766.

DOI: https://doi.org/10.1042/BCJ20210741

Published: 28 March 2022

.... Parkin activation involves binding of a phosphorylated ubiquitin (pUb), followed by phosphorylation of the Ubl domain in parkin, both mediated by the OMM kinase, PINK1. How an OMM protein is selected for ubiquitination is unclear. Parkin targeted OMM proteins have little structural or sequence similarity...

View article titled, Distinct phosphorylation signals drive acceptor versus free ubiquitin chain targeting by parkin

Includes: Supplementary data

Articles

Conformational plasticity of the ULK3 kinase domain

Sebastian Mathea, Eidarus Salah, Cynthia Tallant, Deep Chatterjee, Benedict-Tilman Berger, Rebecca Konietzny, Susanne Müller, Benedikt M. Kessler, Stefan Knapp

Biochem J (2021) 478 (14): 2811–2823.

DOI: https://doi.org/10.1042/BCJ20210257

Published: 23 July 2021

... conformational changes enzyme–substrate interactions phosphorylation small-molecule inhibitor ULK kinase Membrane abscission is the ultimate step in several physiologically important processes such as exosome budding and cytokinesis [ 1 ]. Any connection between two membrane substructures is cut...

View article titled, Conformational plasticity of the ULK3 kinase domain

Includes: Supplementary data

Articles

Deciphering the LRRK code: LRRK1 and LRRK2 phosphorylate distinct Rab proteins and are regulated by diverse mechanisms

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Protein structure and function

Asad U. Malik, Athanasios Karapetsas, Raja S. Nirujogi, Sebastian Mathea, Deep Chatterjee, Prosenjit Pal, Pawel Lis, Matthew Taylor, Elena Purlyte, Robert Gourlay, Mark Dorward, Simone Weidlich, Rachel Toth, Nicole K. Polinski, Stefan Knapp, Francesca Tonelli, Dario R. Alessi

Biochem J (2021) 478 (3): 553–578.

DOI: https://doi.org/10.1042/BCJ20200937

Published: 10 February 2021

... mutations in LRRK2 that enhance kinase activity cause Parkinson's disease. LRRK2 phosphorylates a subset of Rab GTPases including Rab8A and Rab10 within its effector binding motif. Here, we explore whether LRRK1, a less studied homolog of LRRK2 that regulates growth factor receptor trafficking...

View article titled, Deciphering the LRRK code: LRRK1 and LRRK2 phosphorylate distinct Rab proteins and are regulated by diverse mechanisms

Includes: Supplementary data

Articles

Structural insights into DNA double-strand break signaling

Rashmi Panigrahi, J. N. Mark Glover

Biochem J (2021) 478 (1): 135–156.

DOI: https://doi.org/10.1042/BCJ20200066

Published: 13 January 2021

... of the Biochemical Society 2021 DNA damage signaling mediators phosphorylation sensors ubiquitylation BRCA1 is a multidomain protein of 1863 amino acids that is critical for DSB repair via homologous recombination. Mutations in BRCA1 are associated with a pronounced predisposition...

View article titled, Structural insights into DNA double-strand break signaling

Articles

PARP-1 activation after oxidative insult promotes energy stress-dependent phosphorylation of YAP1 and reduces cell viability

Sandra M. Martín-Guerrero, Pedro Casado, Maruan Hijazi, Vinothini Rajeeve, Julio Plaza-Díaz, Francisco Abadía-Molina, Julio Navascués, Miguel A. Cuadros, Pedro R. Cutillas, David Martín-Oliva

Biochem J (2020) 477 (23): 4491–4513.

DOI: https://doi.org/10.1042/BCJ20200525

Published: 03 December 2020

...-based phosphoproteomics in WRL68 cells showed that the oxidative damage induced by H 2 O 2 increased the phosphorylation of YAP1, a transcriptional co-activator involved in cell survival, and modified the phosphorylation of other proteins involved in transcription. Genetic or pharmacological inhibition...

View article titled, PARP-1 activation after oxidative insult promotes energy stress-dependent phosphorylation of YAP1 and reduces cell viability

Includes: Supplementary data

Articles

RORα phosphorylation by casein kinase 1α as glucose signal to regulate estrogen sulfation in human liver cells

Hao Hu, Masahiko Negishi

Biochem J (2020) 477 (18): 3583–3598.

DOI: https://doi.org/10.1042/BCJ20200427

Published: 28 September 2020

... HepG2 cells cultured in high glucose (450 mg/dl) medium. Here, we have investigated this glucose signal that leads to phosphorylation of nuclear receptor RORα (NR1F1) at Ser100 and the transcription mechanism by which phosphorylated RORα transduces this signal to nuclear receptor HNF4α, activating...

View article titled, RORα phosphorylation by casein kinase 1α as glucose signal to regulate estrogen sulfation in human liver cells

Includes: Supplementary data

Articles

AMP-activated protein kinase regulates alternative pre-mRNA splicing by phosphorylation of SRSF1

Eri Matsumoto, Kaho Akiyama, Takuya Saito, Yu Matsumoto, Ken-Ichi Kobayashi, Jun Inoue, Yuji Yamamoto, Tsukasa Suzuki

Biochem J (2020) 477 (12): 2237–2248.

DOI: https://doi.org/10.1042/BCJ20190894

Published: 24 June 2020

... substrate. AMPK directly phosphorylated SRSF1 at Ser133 in an RNA recognition motif. Ser133 phosphorylation suppressed the interaction between SRSF1 and specific RNA sequences without altering the subcellular localization of SRSF1. Moreover, AMPK regulated the SRSF1-mediated alternative pre-mRNA splicing...

View article titled, AMP-activated protein kinase regulates alternative pre-mRNA splicing by phosphorylation of SRSF1

Articles

Reading the phosphorylation code: binding of the 14-3-3 protein to multivalent client phosphoproteins

Nikolai N. Sluchanko

Biochem J (2020) 477 (7): 1219–1225.

DOI: https://doi.org/10.1042/BCJ20200084

Published: 09 April 2020

...Nikolai N. Sluchanko Many major protein–protein interaction networks are maintained by ‘hub’ proteins with multiple binding partners, where interactions are often facilitated by intrinsically disordered protein regions that undergo post-translational modifications, such as phosphorylation...

View article titled, Reading the phosphorylation code: binding of the 14-3-3 protein to multivalent client phosphoproteins

Articles

Ufd1 phosphorylation at serine 229 negatively regulates endoplasmic reticulum-associated degradation by inhibiting the interaction of Ufd1 with VCP

Quynh-Anh Thi Nguyen, Juyong Choi, Jin Kuk Yang, Sang Yoon Lee

Biochem J (2019) 476 (18): 2561–2577.

DOI: https://doi.org/10.1042/BCJ20190254

Published: 20 September 2019

... degradation protein 1 (Ufd1) with VCP via its SHP box motif ( 228 F-S-G-S-G-N-R-L 235 ) is required for ERAD. However, the mechanisms by which the VCP–Ufd1 interaction is regulated are not well understood. Here, we found that the serine 229 residue located in the Ufd1 SHP box is phosphorylated in vitro...

View article titled, Ufd1 phosphorylation at serine 229 negatively regulates endoplasmic reticulum-associated degradation by inhibiting the interaction of Ufd1 with VCP

Articles

RhoBTB1 interacts with ROCKs and inhibits invasion

Raquel B. Haga, Ritu Garg, Francesca Collu, Bárbara Borda D'Agua, Sofia T. Menéndez, Audrey Colomba, Franca Fraternali, Anne J. Ridley

Biochem J (2019) 476 (17): 2499–2514.

DOI: https://doi.org/10.1042/BCJ20190203

Published: 13 September 2019

... with ROCK1 is via its Rho domain. The Rho domain binds to the coiled-coil region of ROCK1 close to its kinase domain. We identify two amino acids within the Rho domain that alter RhoBTB1 association with ROCK1. RhoBTB1 is a substrate for ROCK1, and mutation of putative phosphorylation sites reduces its...

View article titled, RhoBTB1 interacts with ROCKs and inhibits invasion

Includes: Supplementary data

Articles

Nitration-induced ubiquitination and degradation control quality of ERK1

Yuanya Zhang, Xiahe Huang, Jinlong Wang, Xiaorong Wang, Xiaofei Liu, Yuhang Chen, Wu Xu, Yingchun Wang

Biochem J (2019) 476 (13): 1911–1926.

DOI: https://doi.org/10.1042/BCJ20190240

Published: 02 July 2019

... License 4.0 (CC BY) . ERK mass spectrometry phosphorylation quality control tyrosine nitration ubiquitination The mitogen-activate protein kinase ERKs (extracellular-regulated protein kinases) play a central role in various cellular processes, including proliferation, migration...

View article titled, Nitration-induced ubiquitination and degradation control quality of ERK1

Includes: Supplementary data

Articles

G protein subunit phosphorylation as a regulatory mechanism in heterotrimeric G protein signaling in mammals, yeast, and plants

David Chakravorty, Sarah M. Assmann

Biochem J (2018) 475 (21): 3331–3357.

DOI: https://doi.org/10.1042/BCJ20160819

Published: 09 November 2018

... are fundamental to human health [ Biochimica et Biophysica Acta (2007) 1768 , 994–1005] and are the target of >30% of pharmaceuticals in clinical use [ Biotechnology Advances (2013) 31 , 1676–1694; Nature Reviews Drug Discovery (2017) 16 , 829–842]. This review focuses on phosphorylation of G protein subunits...

View article titled, G protein subunit phosphorylation as a regulatory mechanism in heterotrimeric G protein signaling in mammals, yeast, and plants

Includes: Supplementary data

Articles

PKA-site phosphorylation of importin13 regulates its subcellular localization and nuclear transport function

Xujie Liu, Wenbo Lin, Xiuyu Shi, Rebecca G. Davies, Kylie M. Wagstaff, Tao Tao, David A. Jans

Biochem J (2018) 475 (16): 2699–2712.

DOI: https://doi.org/10.1042/BCJ20180082

Published: 31 August 2018

... to undergo phosphorylation, but the impact of this on function has not been investigated. Here, we show for the first time that IPO13 is phosphorylated by cAMP-dependent protein kinase A specifically at serine 193. Results from fluorescence recovery after photobleaching and fluorescence loss...

View article titled, PKA-site phosphorylation of importin13 regulates its subcellular localization and nuclear transport function

Articles

The Parkinson's disease VPS35[D620N] mutation enhances LRRK2-mediated Rab protein phosphorylation in mouse and human

In Collection

Editors' pick of research highlights published in the Biochemical Journal in 2018 & 2019

Rafeeq Mir, Francesca Tonelli, Pawel Lis, Thomas Macartney, Nicole K. Polinski, Terina N. Martinez, Meng-Yun Chou, Andrew J.M. Howden, Theresa König, Christoph Hotzy, Ivan Milenkovic, Thomas Brücke, Alexander Zimprich, Esther Sammler, Dario R. Alessi

Biochem J (2018) 475 (11): 1861–1883.

DOI: https://doi.org/10.1042/BCJ20180248

Published: 06 June 2018

... repeat protein kinase-2) and VPS35 genes result in autosomal dominant Parkinson's disease. The VPS35 gene encodes for the cargo-binding component of the retromer complex, while LRRK2 modulates vesicular trafficking by phosphorylating a subgroup of Rab proteins. Pathogenic mutations in LRRK2 increase its...

View article titled, The Parkinson's disease VPS35[D620N] mutation enhances LRRK2-mediated Rab protein phosphorylation in mouse and human

Includes: Supplementary data

Articles

Biological role of site-specific O-glycosylation in cell adhesion activity and phosphorylation of osteopontin

Midori Oyama, Yoshinobu Kariya, Yukiko Kariya, Kana Matsumoto, Mayumi Kanno, Yoshiki Yamaguchi, Yasuhiro Hashimoto

Biochem J (2018) 475 (9): 1583–1595.

DOI: https://doi.org/10.1042/BCJ20170205

Published: 09 May 2018

... lacking five O-glycosylation sites (Thr 134 /Thr 138 /Thr 143 /Thr 147 /Thr 152 ) in the threonine/proline-rich region increased cell adhesion activity and phosphorylation compared with the wild type. However, the role of O-glycosylation in cell adhesion activity and phosphorylation of OPN remains...

View article titled, Biological role of site-specific O-glycosylation in cell adhesion activity and phosphorylation of osteopontin

Includes: Supplementary data

Articles

Phosphorylation of BACH1 switches its function from transcription factor to mitotic chromosome regulator and promotes its interaction with HMMR

Jie Li, Hiroki Shima, Hironari Nishizawa, Masatoshi Ikeda, Andrey Brydun, Mitsuyo Matsumoto, Hiroki Kato, Yuriko Saiki, Liang Liu, Miki Watanabe-Matsui, Kenji Iemura, Kozo Tanaka, Takuma Shiraki, Kazuhiko Igarashi

Biochem J (2018) 475 (5): 981–1002.

DOI: https://doi.org/10.1042/BCJ20170520

Published: 15 March 2018

... interactions with proteins involved in chromatin and gene expression but retained interactions with HMMR and its known partners including CHICA. By analyzing BACH1 modification using stable isotope labeling with amino acids in cell culture, mitosis-specific phosphorylations of BACH1 were observed...

View article titled, Phosphorylation of BACH1 switches its function from transcription factor to mitotic chromosome regulator and promotes its interaction with HMMR

Articles

Back to the future: new target-validated Rab antibodies for evaluating LRRK2 signalling in cell biology and Parkinson's disease

Patrick A. Eyers

Biochem J (2018) 475 (1): 185–189.

DOI: https://doi.org/10.1042/BCJ20170870

Published: 05 January 2018

... (LRRK2) is a Ser/Thr kinase linked to familial and sporadic cases of Parkinson's disease (PD). Recent work established that multiple Rab GTPases are physiological substrates of LRRK2, with Rab10 in particular emerging as a human substrate whose site-specific phosphorylation mirrors hyperactive LRRK2...

View article titled, Back to the future: new target-validated Rab antibodies for evaluating LRRK2 signalling in cell biology and Parkinson's disease

Articles

Dynamic multi-site phosphorylation by Fyn and Abl drives the interaction between CRKL and the novel scaffolding receptors DCBLD1 and DCBLD2

Anna M. Schmoker, Jaye L. Weinert, Kyle J. Kellett, Hannah E. Johnson, Ryan M. Joy, Marion E. Weir, Alicia M. Ebert, Bryan A. Ballif

Biochem J (2017) 474 (23): 3963–3984.

DOI: https://doi.org/10.1042/BCJ20170615

Published: 21 November 2017

... the conserved signaling features of DCBLD family members that drive their molecular activities. We previously identified DCBLD2 tyrosine phosphorylation sites in intracellular YxxP motifs that are required for the phosphorylation-dependent binding of the signaling adaptors CRK and CRKL (CT10 regulator of kinase...

View article titled, Dynamic multi-site phosphorylation by Fyn and Abl drives the interaction between CRKL and the novel scaffolding receptors DCBLD1 and DCBLD2

Includes: Supplementary data

Articles

Reactive sulfur species inactivate Ca 2+ /calmodulin-dependent protein kinase IV via S-polysulfidation of its active-site cysteine residue

Tsuyoshi Takata, Hideshi Ihara, Naoya Hatano, Yukihiro Tsuchiya, Takaaki Akaike, Yasuo Watanabe

Biochem J (2017) 474 (15): 2547–2562.

DOI: https://doi.org/10.1042/BCJ20170092

Published: 18 July 2017

... inactivated by RSS via polysulfidation of the active-site Cys residue. CaMKIV is phosphorylated at Thr 196 by its upstream CaMK kinase (CaMKK), resulting in the induction of its full activity. In vitro incubation of CaMKIV with the exogenous RSS donors Na 2 S n ( n = 2–4) resulted in dose-dependent inhibition...

View article titled, Reactive sulfur species inactivate Ca 2+ /calmodulin-dependent protein kinase IV via S-polysulfidation of its active-site cysteine residue

Includes: Supplementary data

Articles

HIV-1 Tat potently stabilises Mdm2 and enhances viral replication

Rameez Raja, Larance Ronsard, Sneh Lata, Shubhendu Trivedi, Akhil C. Banerjea

Biochem J (2017) 474 (14): 2449–2464.

DOI: https://doi.org/10.1042/BCJ20160825

Published: 11 July 2017

... and its implications for viral replication have not been well studied. Here, we show that the Mdm2 protein level increases during HIV-1 infection and this effect is mediated by HIV-1 Tat protein. Tat appears to stabilise Mdm2 at the post-translational level by inducing its phosphorylation at serine-166...

View article titled, HIV-1 Tat potently stabilises Mdm2 and enhances viral replication

Includes: Supplementary data

Articles

A role for prolyl isomerase PIN1 in the phosphorylation-dependent modulation of PRRXL1 function

Ricardo Soares-dos-Reis, Ana Sofia Pessoa, Ana Filipa Dias, Miguel Falcão, Mariana Raimundo Matos, Rui Vitorino, Filipe Almeida Monteiro, Deolinda Lima, Carlos Reguenga

Biochem J (2017) 474 (5): 683–697.

DOI: https://doi.org/10.1042/BCJ20160560

Published: 20 February 2017

... highly conserved phosphorylation sites (T110, S119, S231, S233 and S251) in PRRXL1 primary structure. Four are phospho-S/T-P sites, which suggest a role for the prolyl isomerase PIN1 in regulating PRRXL1. Accordingly, PRRXL1 physically interacts with PIN1 and displays diminished transcriptional activity...

View article titled, A role for prolyl isomerase PIN1 in the phosphorylation-dependent modulation of PRRXL1 function

Articles

Structure and inhibitor specificity of the PCTAIRE-family kinase CDK16

Sarah E. Dixon-Clarke, Saifeldin N. Shehata, Tobias Krojer, Timothy D. Sharpe, Frank von Delft, Kei Sakamoto, Alex N. Bullock

Biochem J (2017) 474 (5): 699–713.

DOI: https://doi.org/10.1042/BCJ20160941

Published: 20 February 2017

... trafficking and cancer cell proliferation. CDK16 is activated through binding to cyclin Y via a phosphorylation-dependent 14-3-3 interaction and has a unique consensus substrate phosphorylation motif compared with conventional CDKs. To elucidate the structure and inhibitor-binding properties of this atypical...

View article titled, Structure and inhibitor specificity of the PCTAIRE-family kinase CDK16

Includes: Supplementary data

Articles

Identification of key phosphorylation sites in PTH1R that determine arrestin3 binding and fine-tune receptor signaling

Diana Zindel, Sandra Engel, Andrew R. Bottrill, Jean-Philippe Pin, Laurent Prézeau, Andrew B. Tobin, Moritz Bünemann, Cornelius Krasel, Adrian J. Butcher

Biochem J (2016) 473 (22): 4173–4192.

DOI: https://doi.org/10.1042/BCJ20160740

Published: 10 November 2016

... and kidney where it modulates extracellular Ca 2+ homeostasis and bone turnover. It is well established that phosphorylation of GPCRs constitutes a key event in regulating receptor function by promoting arrestin recruitment and coupling to G-protein-independent signaling pathways. Mapping phosphorylation...

View article titled, Identification of key phosphorylation sites in PTH1R that determine arrestin3 binding and fine-tune receptor signaling

Articles

The interaction between AMPKβ2 and the PP1-targeting subunit R6 is dynamically regulated by intracellular glycogen content

Yvonne Oligschlaeger, Marie Miglianico, Vivian Dahlmans, Carla Rubio-Villena, Dipanjan Chanda, Maria Adelaida Garcia-Gimeno, Will A. Coumans, Yilin Liu, J. Willem Voncken, Joost J.F.P. Luiken, Jan F.C. Glatz, Pascual Sanz, Dietbert Neumann

Biochem J (2016) 473 (7): 937–947.

DOI: https://doi.org/10.1042/BJ20151035

Published: 29 March 2016

... the glucose-induced inactivation of AMPK. In the present study, we further investigated the interaction of R6 with AMPKβ and the possible dependency on Thr-148 phosphorylation status. Yeast two-hybrid (Y2H) analyses and co-immunoprecipitation (IP) of the overexpressed proteins in human embryonic kidney (HEK...

View article titled, The interaction between AMPKβ2 and the PP1-targeting subunit R6 is dynamically regulated by intracellular glycogen content

Articles

Protein kinase Cζ exhibits constitutive phosphorylation and phosphatidylinositol-3,4,5-triphosphate-independent regulation

Irene S. Tobias, Manuel Kaulich, Peter K. Kim, Nitya Simon, Estela Jacinto, Steven F. Dowdy, Charles C. King, Alexandra C. Newton

Biochem J (2016) 473 (4): 509–523.

DOI: https://doi.org/10.1042/BJ20151013

Published: 09 February 2016

... that aPKC is constitutively phosphorylated and, using a genetically-encoded reporter for PKC activity, basally active in cells. Specifically, we show that phosphorylation at two key regulatory sites, the activation loop and turn motif, of the aPKC PKCζ in multiple cultured cell types is constitutive...

View article titled, Protein kinase Cζ exhibits constitutive phosphorylation and phosphatidylinositol-3,4,5-triphosphate-independent regulation

Articles

A novel phosphorylation site at Ser 130 adjacent to the pseudosubstrate domain contributes to the activation of protein kinase C-δ

Jianli Gong, Ronald J. Holewinski, Jennifer E. Van Eyk, Susan F. Steinberg

Biochem J (2016) 473 (3): 311–320.

DOI: https://doi.org/10.1042/BJ20150812

Published: 25 January 2016

... phosphorylation [Gong et al. (2015) Mol. Cell. Biol. 35 , 1727–1740]. The present study uses MS-based methods to identify PKCδ phosphorylation at Thr 50 and Ser 645 (in resting and PMA-treated cardiomyocytes) as well as Thr 37 , Thr 38 , Ser 130 , Thr 164 , Thr 211 , Thr 215 , Ser 218 , Thr 295 , Ser 299 and Thr...

View article titled, A novel phosphorylation site at Ser 130 adjacent to the pseudosubstrate domain contributes to the activation of protein kinase C-δ

Articles

Nuclear protein kinase CLK1 uses a non-traditional docking mechanism to select physiological substrates

Malik M. Keshwani, Kendra L. Hailey, Brandon E. Aubol, Laurent Fattet, Maria L. McGlone, Patricia A. Jennings, Joseph A. Adams

Biochem J (2015) 472 (3): 329–338.

DOI: https://doi.org/10.1042/BJ20150903

Published: 27 November 2015

...Malik M. Keshwani; Kendra L. Hailey; Brandon E. Aubol; Laurent Fattet; Maria L. McGlone; Patricia A. Jennings; Joseph A. Adams Phosphorylation-dependent cell communication requires enzymes that specifically recognize key proteins in a sea of similar, competing substrates. The protein kinases...

View article titled, Nuclear protein kinase CLK1 uses a non-traditional docking mechanism to select physiological substrates

Articles

MyelStones: the executive roles of myelin basic protein in myelin assembly and destabilization in multiple sclerosis

Kenrick A. Vassall, Vladimir V. Bamm, George Harauz

Biochem J (2015) 472 (1): 17–32.

DOI: https://doi.org/10.1042/BJ20150710

Published: 30 October 2015

... fragments (MoRFs), which thereby undergo local disorder-to-order transitions. Their conformations and associations are modulated by environment and by a dynamic barcode of post-translational modifications, particularly phosphorylation by mitogen-activated and other protein kinases and deimination...

View article titled, MyelStones: the executive roles of myelin basic protein in myelin assembly and destabilization in multiple sclerosis

Articles

The NHERF2 sequence adjacent and upstream of the ERM-binding domain affects NHERF2–ezrin binding and dexamethasone stimulated NHE3 activity

Jianbo Yang, Rafiquel Sarker, Varsha Singh, Prateeti Sarker, Jianyi Yin, Tian-E Chen, Raghothama Chaerkady, Xuhang Li, C. Ming Tse, Mark Donowitz

Biochem J (2015) 470 (1): 77–90.

DOI: https://doi.org/10.1042/BJ20150238

Published: 06 August 2015

... exclusively to the apical domain. Furthermore, phosphorylation of Ser 303 located in the EBRS of NHERF2, decreases the binding affinity for ezrin, dislocates apical NHERF2 into the cytosol and increases the NHERF2 microvillar mobility rate. Moreover, increased phosphorylation of Ser 303 was functionally...

View article titled, The NHERF2 sequence adjacent and upstream of the ERM-binding domain affects NHERF2–ezrin binding and dexamethasone stimulated NHE3 activity

Articles

Akt-mediated regulation of antidepressant-sensitive serotonin transporter function, cell-surface expression and phosphorylation

Jeyaganesh Rajamanickam, Balasubramaniam Annamalai, Troels Rahbek-Clemmensen, Santhanalakshmi Sundaramurthy, Ulrik Gether, Lankupalle D. Jayanthi, Sammanda Ramamoorthy

Biochem J (2015) 468 (1): 177–190.

DOI: https://doi.org/10.1042/BJ20140826

Published: 05 May 2015

... and phosphorylation. However, whether Akt/PKB (protein kinase) regulates SERT function is not known. In the present study, we made the novel observation that inhibition of Akt resulted in the down-regulation of SERT function through the regulation of SERT trafficking and phosphorylation. Akt inhibitor Akt X {10-(4...

View article titled, Akt-mediated regulation of antidepressant-sensitive serotonin transporter function, cell-surface expression and phosphorylation

Articles

Conserved proline-directed phosphorylation regulates SR protein conformation and splicing function

Malik M. Keshwani, Brandon E. Aubol, Laurent Fattet, Chen-Ting Ma, Jinsong Qiu, Patricia A. Jennings, Xiang-Dong Fu, Joseph A. Adams

Biochem J (2015) 466 (2): 311–322.

DOI: https://doi.org/10.1042/BJ20141373

Published: 20 February 2015

... in arginine–serine dipeptide repeats (RS domains). Although the SRPKs (SR-specific protein kinases) phosphorylate these repeats, RS domains also contain prolines with flanking serines that are phosphorylated by a second family of protein kinases known as the CLKs (Cdc2-like kinases). The role of specific...

View article titled, Conserved proline-directed phosphorylation regulates SR protein conformation and splicing function

Includes: Supplementary data

Articles

A protein kinase screen of Neurospora crassa mutant strains reveals that the SNF1 protein kinase promotes glycogen synthase phosphorylation

Thiago De Souza Candido, Rodrigo Duarte Gonçalves, Ana Paula Felício, Fernanda Zanolli Freitas, Fernanda Barbosa Cupertino, Ana Carolina Gomes Vieira De Carvalho, Maria Célia Bertolini

Biochem J (2014) 464 (3): 323–334.

DOI: https://doi.org/10.1042/BJ20140942

Published: 05 December 2014

.... The activities of glycogen synthase and glycogen phosphorylase, the rate-limiting enzymes of the synthesis and degradation processes, respectively, are regulated by allosteric modulation and reversible phosphorylation. To identify the protein kinases affecting glycogen metabolism in Neurospora crassa , we...

View article titled, A protein kinase screen of Neurospora crassa mutant strains reveals that the SNF1 protein kinase promotes glycogen synthase phosphorylation

Includes: Supplementary data

Articles

PI4KIIα phosphorylation by GSK3 directs vesicular trafficking to lysosomes

James W. Robinson, Iryna Leshchyns’ka, Hovik Farghaian, William E. Hughes, Vladimir Sytnyk, Graham G. Neely, Adam R. Cole

Biochem J (2014) 464 (1): 145–156.

DOI: https://doi.org/10.1042/BJ20140497

Published: 23 October 2014

... phosphorylates two distinct sites in the N-terminus of PI4KIIα (Ser 5 and Ser 47 ), promoting binding to the adaptor protein 3 (AP-3) complex for trafficking to the lysosome to be degraded. Blocking phosphorylation reduces trafficking to the lysosome, stabilizing PI4KIIα and its cargo proteins for redistribution...

View article titled, PI4KIIα phosphorylation by GSK3 directs vesicular trafficking to lysosomes

Articles

Priming IKKβ kinase for action

Steven C. Ley, Rudi Beyaert

Biochem J (2014) 463 (1): e1–e2.

DOI: https://doi.org/10.1042/BJ20140989

Published: 08 September 2014

..., activation of IKKβ requires phosphorylation of the activation loop of its kinase domain. Different upstream protein kinases, and IKKβ itself, have been reported to directly phosphorylate and activate IKKβ in vitro , but the exact molecular mechanism of IKKβ activation in cells has remained unclear...

View article titled, Priming IKKβ kinase for action

Articles

Osteopontin O -glycosylation contributes to its phosphorylation and cell-adhesion properties

Yoshinobu Kariya, Mayumi Kanno, Kana Matsumoto-Morita, Midori Konno, Yoshiki Yamaguchi, Yasuhiro Hashimoto

Biochem J (2014) 463 (1): 93–102.

DOI: https://doi.org/10.1042/BJ20140060

Published: 08 September 2014

... and adhesion primarily through its association with several integrins such as αvβ3, and its phosphorylation affects these processes. However, the mechanism by which OPN O -glycosylation affects these processes is not completely understood. In the present study, we demonstrated that OPN O -glycosylation self...

View article titled, Osteopontin O -glycosylation contributes to its phosphorylation and cell-adhesion properties

Includes: Supplementary data

Articles

Regulation of PKA activity by an autophosphorylation mechanism in Saccharomyces cerevisiae

Clara Andrea Solari, Vanesa Tudisca, Marcelo Pugliessi, Alejandro Daniel Nadra, Silvia Moreno, Paula Portela

Biochem J (2014) 462 (3): 567–579.

DOI: https://doi.org/10.1042/BJ20140577

Published: 22 August 2014

...Clara Andrea Solari; Vanesa Tudisca; Marcelo Pugliessi; Alejandro Daniel Nadra; Silvia Moreno; Paula Portela PKA (cAMP-dependent protein kinase) activity, as well as that of other AGC members, is regulated by multiple phosphorylations of its catalytic subunits. In Saccharomyces cerevisiae , the PKA...

View article titled, Regulation of PKA activity by an autophosphorylation mechanism in Saccharomyces cerevisiae

Includes: Supplementary data

Articles

N-terminus of the protein kinase CLK1 induces SR protein hyperphosphorylation

Brandon E. Aubol, Ryan M. Plocinik, Malik M. Keshwani, Maria L. McGlone, Jonathan C. Hagopian, Gourisankar Ghosh, Xiang-Dong Fu, Joseph A. Adams

Biochem J (2014) 462 (1): 143–152.

DOI: https://doi.org/10.1042/BJ20140494

Published: 24 July 2014

...Brandon E. Aubol; Ryan M. Plocinik; Malik M. Keshwani; Maria L. McGlone; Jonathan C. Hagopian; Gourisankar Ghosh; Xiang-Dong Fu; Joseph A. Adams SR proteins are essential splicing factors that are regulated through multisite phosphorylation of their RS (arginine/serine-rich) domains by two major...

View article titled, N-terminus of the protein kinase CLK1 induces SR protein hyperphosphorylation

Includes: Supplementary data

Articles

T-cell co-stimulation through the CD2 and CD28 co-receptors induces distinct signalling responses

Sigrid S. Skånland, Kristine Moltu, Torunn Berge, Einar M. Aandahl, Kjetil Taskén

Biochem J (2014) 460 (3): 399–410.

DOI: https://doi.org/10.1042/BJ20140040

Published: 29 May 2014

... that CD2 co-stimulation induces phosphorylation of the TCR-proximal signalling complex, whereas CD28 activates distal signalling molecules, including the transcription factors NF-κB (nuclear factor κB), ATF (activating transcription factor)-2, STAT3/5 (signal transducer and activator of transcription 3/5...

View article titled, T-cell co-stimulation through the CD2 and CD28 co-receptors induces distinct signalling responses

Includes: Supplementary data

Articles

Kinase and channel activity of TRPM6 are co-ordinated by a dimerization motif and pocket interaction

Jenny van der Wijst, Maxime G. Blanchard, Helen I. Woodroof, Thomas J. Macartney, Robert Gourlay, Joost G. Hoenderop, René J. Bindels, Dario R. Alessi

Biochem J (2014) 460 (2): 165–175.

DOI: https://doi.org/10.1042/BJ20131639

Published: 13 May 2014

... through a kinase-independent mechanism involving the dimerization motif binding to a pocket within the kinase domain. A disease-causing mutation (S1754N) lying nearby the dimerization pocket inactivates kinase activity. dimerization motif hypomagnesaemia ion channel phosphorylation protein...

View article titled, Kinase and channel activity of TRPM6 are co-ordinated by a dimerization motif and pocket interaction

Includes: Supplementary data

Articles

Parkin is activated by PINK1-dependent phosphorylation of ubiquitin at Ser 65

Agne Kazlauskaite, Chandana Kondapalli, Robert Gourlay, David G. Campbell, Maria Stella Ritorto, Kay Hofmann, Dario R. Alessi, Axel Knebel, Matthias Trost, Miratul M. K. Muqit

Biochem J (2014) 460 (1): 127–141.

DOI: https://doi.org/10.1042/BJ20140334

Published: 25 April 2014

...) is activated by mitochondrial depolarization and stimulates the Parkin E3 ligase by phosphorylating Ser 65 within its Ubl (ubiquitin-like) domain. Using phosphoproteomic analysis, we identified a novel ubiquitin phosphopeptide phosphorylated at Ser 65 that was enriched 14-fold in HEK (human embryonic kidney...

View article titled, Parkin is activated by PINK1-dependent phosphorylation of ubiquitin at Ser 65

Includes: Supplementary data

Articles

Ser 119 phosphorylation modulates the activity and conformation of PRRXL1, a homeodomain transcription factor

Ricardo Soares-dos-Reis, Ana S. Pessoa, Mariana R. Matos, Miguel Falcão, Vera M. Mendes, Bruno Manadas, Filipe A. Monteiro, Deolinda Lima, Carlos Reguenga

Biochem J (2014) 459 (3): 441–453.

DOI: https://doi.org/10.1042/BJ20131014

Published: 11 April 2014

... expressed in DRG and dSC (dorsal spinal cord) nociceptive neurons. PRRXL1 is crucial for the establishment and maintenance of nociceptive circuitry, as Prrxl1 −/− mice present neuronal loss, reduced pain sensitivity and failure to thrive. In the present study, we show that PRRXL1 is highly phosphorylated...

View article titled, Ser 119 phosphorylation modulates the activity and conformation of PRRXL1, a homeodomain transcription factor

Includes: Supplementary data

Articles

Redox signal regulation via nNOS phosphorylation at Ser 847 in PC12 cells and rat cerebellar granule neurons

Shingo Kasamatsu, Yasuo Watanabe, Tomohiro Sawa, Takaaki Akaike, Hideshi Ihara

Biochem J (2014) 459 (2): 251–263.

DOI: https://doi.org/10.1042/BJ20131262

Published: 28 March 2014

...Shingo Kasamatsu; Yasuo Watanabe; Tomohiro Sawa; Takaaki Akaike; Hideshi Ihara Phosphorylation is considered a main mechanism modulating nNOS (neuronal nitric oxide synthase) function to reduce NO production. In the present study, the effects of nNOS phosphorylation on redox signalling, including...

View article titled, Redox signal regulation via nNOS phosphorylation at Ser 847 in PC12 cells and rat cerebellar granule neurons

Articles

Stability of the human pregnane X receptor is regulated by E3 ligase UBR5 and serine/threonine kinase DYRK2

Su Sien Ong, Asli N. Goktug, Ayesha Elias, Jing Wu, Darren Saunders, Taosheng Chen

Biochem J (2014) 459 (1): 193–203.

DOI: https://doi.org/10.1042/BJ20130558

Published: 14 March 2014

... enzymes. To date, little is known about the upstream regulation of hPXR. Using MS analysis and a kinome-wide siRNA screen, we report that the E3 ligase UBR5 (ubiquitin protein ligase E3 component n-recognin 5) and DYRK2 (dual-specificity tyrosine-phosphorylation-regulated kinase 2) regulate hPXR stability...

View article titled, Stability of the human pregnane X receptor is regulated by E3 ligase UBR5 and serine/threonine kinase DYRK2

Includes: Supplementary data

Articles

Phosphorylation of Arabidopsis transketolase at Ser 428 provides a potential paradigm for the metabolic control of chloroplast carbon metabolism

Agostinho G. Rocha, Norbert Mehlmer, Simon Stael, Andrea Mair, Nargis Parvin, Fatima Chigri, Markus Teige, Ute C. Vothknecht

Biochem J (2014) 458 (2): 313–322.

DOI: https://doi.org/10.1042/BJ20130631

Published: 14 February 2014

... the targets of calcium-dependent phosphorylation within the stromal proteome. A 73 kDa protein was identified as one of the most dominant proteins undergoing phosphorylation in a calcium-dependent manner in the stromal extracts of both Arabidopsis and Pisum . It was identified as TKL (transketolase...

View article titled, Phosphorylation of Arabidopsis transketolase at Ser 428 provides a potential paradigm for the metabolic control of chloroplast carbon metabolism

Includes: Supplementary data

Articles

Mechanistic insights into activation and SOCS3-mediated inhibition of myeloproliferative neoplasm-associated JAK2 mutants from biochemical and structural analyses

Leila N. Varghese, Daniela Ungureanu, Nicholas P. D. Liau, Samuel N. Young, Artem Laktyushin, Henrik Hammaren, Isabelle S. Lucet, Nicos A. Nicola, Olli Silvennoinen, Jeffrey J. Babon, James M. Murphy

Biochem J (2014) 458 (2): 395–405.

DOI: https://doi.org/10.1042/BJ20131516

Published: 14 February 2014

... is the phosphorylation of Tyr 570 , an event thought to be an inhibitory signal [ 47 , 48 ]. Phosphorylation of Tyr 570 has been suggested to be an autoactivation event catalysed by the pseudokinase (JH2) domain, which is down-regulated in MPN-derived JAK2 mutants [ 12 , 14 ]. Using an antibody specific to phospho-Tyr...

View article titled, Mechanistic insights into activation and SOCS3-mediated inhibition of myeloproliferative neoplasm-associated JAK2 mutants from biochemical and structural analyses

Includes: Supplementary data

Articles

Identification of protein phosphatase 1 as a regulator of the LRRK2 phosphorylation cycle

Evy Lobbestael, Jing Zhao, Iakov N. Rudenko, Aleksandra Beylina, Fangye Gao, Justin Wetter, Monique Beullens, Mathieu Bollen, Mark R. Cookson, Veerle Baekelandt, R. Jeremy Nichols, Jean-Marc Taymans

Biochem J (2013) 456 (1): 119–128.

DOI: https://doi.org/10.1042/BJ20121772

Published: 24 October 2013

...Evy Lobbestael; Jing Zhao; Iakov N. Rudenko; Aleksandra Beylina; Fangye Gao; Justin Wetter; Monique Beullens; Mathieu Bollen; Mark R. Cookson; Veerle Baekelandt; R. Jeremy Nichols; Jean-Marc Taymans A cluster of phosphorylation sites in LRRK2 (leucine-rich repeat kinase 2), including Ser 910 , Ser...

View article titled, Identification of protein phosphatase 1 as a regulator of the LRRK2 phosphorylation cycle

Includes: Supplementary data

Articles

Crystal structures of S6K1 provide insights into the regulation mechanism of S6K1 by the hydrophobic motif

Jianchuan Wang, Chen Zhong, Fang Wang, Fangfang Qu, Jianping Ding

Biochem J (2013) 454 (1): 39–47.

DOI: https://doi.org/10.1042/BJ20121863

Published: 26 July 2013

...Jianchuan Wang; Chen Zhong; Fang Wang; Fangfang Qu; Jianping Ding The activity of S6K1 (p70 ribosomal protein subunit 6 kinase 1) is stimulated by phosphorylation of Thr 389 in the hydrophobic motif by mTORC1 (mammalian target of rapamycin complex 1) and phosphorylation of Thr 229 in the activation...

View article titled, Crystal structures of S6K1 provide insights into the regulation mechanism of S6K1 by the hydrophobic motif

Includes: Supplementary data

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