Lipin family members (lipin 1, 2 and 3) are bi-functional proteins that dephosphorylate PA (phosphatidic acid) to produce DAG (diacylglycerol) and act in the nucleus to regulate gene expression. Although other components of the triacylglycerol synthesis pathway can form oligomeric complexes, it is unknown whether lipin proteins also exist as oligomers. In the present study, using various approaches, we revealed that lipin 1 formed stable homo-oligomers with itself and hetero-oligomers with lipin 2/3. Both the N- and C-terminal regions of lipin 1 mediate its oligomerization in a head-to-head/tail-to-tail manner. We also show that lipin 1 subcellular localization can be influenced through oligomerization, and the individual lipin 1 monomers in the oligomer function independently in catalysing dephosphorylation of PA. The present study provides evidence that lipin proteins function as oligomeric complexes and that the three mammalian lipin isoforms can form combinatorial units.
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Research Article|
October 25 2010
Lipin proteins form homo- and hetero-oligomers
Guang-Hui Liu;
*Institute of Biophysics, Chinese Academy of Sciences, Beijing, China, 100101
3Correspondence may be addressed to either of these authors (email gliu@salk.edu or teh3c@virginia.edu).
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Jing Qu;
Jing Qu
1
*Institute of Biophysics, Chinese Academy of Sciences, Beijing, China, 100101
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Anne E. Carmack;
Anne E. Carmack
†Department of Pharmacology, University of Virginia School of Medicine, Charlottesville, VA 22908, U.S.A.
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Hyun Bae Kim;
Hyun Bae Kim
†Department of Pharmacology, University of Virginia School of Medicine, Charlottesville, VA 22908, U.S.A.
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Chang Chen;
Chang Chen
*Institute of Biophysics, Chinese Academy of Sciences, Beijing, China, 100101
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Hongmei Ren;
Hongmei Ren
‡Department of Cardiovascular Medicine, The Gill Heart Institute, University of Kentucky, Lexington, KY 40536-0509, U.S.A.
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Andrew J. Morris;
Andrew J. Morris
‡Department of Cardiovascular Medicine, The Gill Heart Institute, University of Kentucky, Lexington, KY 40536-0509, U.S.A.
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Brian N. Finck;
Brian N. Finck
§Department of Medicine, Washington University School of Medicine, St. Louis, MO 63110, U.S.A.
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Thurl E. Harris
Thurl E. Harris
3
†Department of Pharmacology, University of Virginia School of Medicine, Charlottesville, VA 22908, U.S.A.
3Correspondence may be addressed to either of these authors (email gliu@salk.edu or teh3c@virginia.edu).
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Publisher: Portland Press Ltd
Received:
April 16 2010
Revision Received:
August 12 2010
Accepted:
August 24 2010
Accepted Manuscript online:
August 24 2010
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2010 Biochemical Society
2010
Biochem J (2010) 432 (1): 65–76.
Article history
Received:
April 16 2010
Revision Received:
August 12 2010
Accepted:
August 24 2010
Accepted Manuscript online:
August 24 2010
Citation
Guang-Hui Liu, Jing Qu, Anne E. Carmack, Hyun Bae Kim, Chang Chen, Hongmei Ren, Andrew J. Morris, Brian N. Finck, Thurl E. Harris; Lipin proteins form homo- and hetero-oligomers. Biochem J 15 November 2010; 432 (1): 65–76. doi: https://doi.org/10.1042/BJ20100584
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