Figure 2.
![(A) The study by Malik et al. demonstrates that PKC phosphorylates at least three sites, Ser1064, Ser1074, and Thr1075, which are located in the CORB domain of LRRK1. Created with BioRender.com. (B) Studying the AlphaFold model of LRRK1 structure, the authors identified that phosphorylation occurs in an unstructured loop region of the CORB domain and propose that phosphorylation stabilizes the CORB resulting in strengthened interactions and ordering of the kinase domain αC helix (Cyan helix in N-lobe). Figure reproduced from [3] under the creative commons license.](https://port.silverchair-cdn.com/port/content_public/journal/biochemj/480/3/10.1042_bcj20220507/1/bcj-2022-0507c.02.png?Expires=1716556046&Signature=Qd0Bt4dadi4Ple~a4rCQgHOnlvMXULfoAHHF6dRLeHS~3slpQc-KgPtouyt-8dDYzqsmzyqElLV1WfVE-9OSWVMpgl76Cwp9wl02tyt0F-afwIkZCwH15tcetd2WXpx~PxJLkzOf9ALtWWCBztvbxKV8v66tn-GkF76Wuf~DUiPtPDt6DSPMxflD3h~Wb9IFrEoslyo6qOCi5pALmDRGhwh5g4298o6-eBkmIo1Y6gjmV9zlIQHqdKBNaJa3izqr-IuxIu-aMv39UjmDcV1lYBnVHuOkxfRAXFjZi3-RwckAf5YVWgoEdq1JWEmMmmanuCsPx4WxLTL4WJtZIjfssw__&Key-Pair-Id=APKAIE5G5CRDK6RD3PGA)
PKC phosphorylates LRRK1 on three residues in the CORB domain, altering its conformation for allosteric regulation of the kinase domain.
(A) The study by Malik et al. demonstrates that PKC phosphorylates at least three sites, Ser1064, Ser1074, and Thr1075, which are located in the CORB domain of LRRK1. Created with BioRender.com. (B) Studying the AlphaFold model of LRRK1 structure, the authors identified that phosphorylation occurs in an unstructured loop region of the CORB domain and propose that phosphorylation stabilizes the CORB resulting in strengthened interactions and ordering of the kinase domain αC helix (Cyan helix in N-lobe). Figure reproduced from [3] under the creative commons license.