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Endogenous Rab38 regulates LRRK2's membrane recruitment and substrate Rab phosphorylation in melanocytes

J Biol Chem . . 2023-10; 
Alexandra Unapanta , Farbod Shavarebi , Jacob Porath , Yiyi Shen , Carson Balen , Albert Nguyen , Josh Tseng , Weng Si Leong , Michelle Liu , Pawel Lis , Santiago M Di Pietro , Annie Hiniker
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Proteins, Expression, Isolation and Analysis Proteins were transferred from gels onto polyvinylidene fluoride membrane (EMD Millipore, IPFL00010) using the Genscript eBlot L1 wet transfer system (cat# L00686). F Get A Quote

摘要

Point mutations in leucine-rich repeat kinase 2 (LRRK2) cause Parkinson's disease and augment LRRK2's kinase activity. However, cellular pathways that endogenously enhance LRRK2 kinase function have not been identified. While overexpressed Rab29 draws LRRK2 to Golgi membranes to increase LRRK2 kinase activity, there is little evidence that endogenous Rab29 performs this function under physiological conditions. Here, we identify Rab38 as a novel physiologic regulator of LRRK2 in melanocytes. In mouse melanocytes, which express high levels of Rab38, Rab32, and Rab29, knockdown (or CRISPR knockout) of Rab38, but not Rab32 or Rab29, decreases phosphorylation of multiple LRRK2 substrates, including Rab10 and Rab12, ... More

关键词

BLOC-3; LRO; LRRK2; Parkinson's disease; Rab10; Rab32; Rab38; melanocytes; melanosomes.