Insights into the cellular consequences of LRRK2-mediated Rab protein phosphorylation

被引:4
作者
Fasiczka, Rachel [1 ]
Naaldijk, Yahaira [1 ]
Brahmia, Besma [1 ]
Hilfiker, Sabine [1 ]
机构
[1] Rutgers New Jersey Med Sch, Dept Anesthesiol, Newark, NJ 07103 USA
关键词
PARKINSONS-DISEASE; KINASE-ACTIVITY; LRRK2; MUTATION; RECRUITMENT; LOCALIZATION; PATHWAY; GTPASE; GOLGI; TRAFFICKING; ACTIVATION;
D O I
10.1042/BST20201145
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Point mutations in leucine-rich repeat kinase 2 (LRRK2) which cause Parkinson's disease increase its kinase activity, and a subset of Rab GTPases have been identified as endogenous LRRK2 kinase substrates. Their phosphorylation correlates with a loss-of function for the membrane trafficking steps they are normally involved in, but it also allows them to bind to a novel set of effector proteins with dominant cellular consequences. In this brief review, we will summarize novel findings related to the LRRK2mediated phosphorylation of Rab GTPases and its various cellular consequences in vitro and in the intact brain, and we will highlight major outstanding questions in the field.
引用
收藏
页码:587 / 595
页数:9
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