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Leucine-Rich Repeat Kinase 2 (LRRK2) pp 145–160Cite as

Regulation of LRRK2 by Phosphatases

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Part of the book series: Advances in Neurobiology ((NEUROBIOL,volume 14))

Abstract

LRRK2 is a highly phosphorylated protein, and evidence of a physiological role for LRRK2 phosphorylation has accumulated in recent years for cellular phosphosites, many of which are found in the ANK-LRR interdomain region, i.e., the S910/S935/S955/S973 sites as well as recently for autophosphorylation sites, at least one of which has been confirmed in cells, S1292. LRRK2 phosphorylation is modulated in several disease or potential therapy relevant conditions such as in disease mutant variants of LRRK2 or following LRRK2 kinase inhibitor treatment. This chapter will focus on the regulation of LRRK2 phosphorylation and more specifically the role of phosphatases in LRRK2 dephosphorylation. This will include reviewing the conditions in which LRRK2 is found to be dephosphorylated, the molecular partners and phosphatases involved in regulating LRRK2 phosphorylation, as well as discussing how LRRK2 phosphatases may be therapeutic targets or biomarkers in their own right.

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The author declares no conflicts of interest.

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Authors and Affiliations

  1. Université de Lille, Inserm, CHU Lille, UMR-S 1172—JPARC Jean-Pierre Aubert Research Center, Neurosciences and Cancer, 1 Place de Verdun, Lille, 59000, France

    Jean-Marc Taymans

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  1. Jean-Marc Taymans
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Correspondence to Jean-Marc Taymans .

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Editors and Affiliations

  1. Biomedical Research Foundation of the Academy of Athens (BRFAA), Athens, Greece

    Hardy J. Rideout

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Taymans, JM. (2017). Regulation of LRRK2 by Phosphatases. In: Rideout, H. (eds) Leucine-Rich Repeat Kinase 2 (LRRK2). Advances in Neurobiology, vol 14. Springer, Cham. https://doi.org/10.1007/978-3-319-49969-7_8

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