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Leucine-rich repeat kinase 2 functionally interacts with microtubules and kinase-dependently modulates cell migration.

Abstract：

:Recent studies indicate that the Parkinson's disease-linked leucine-rich repeat kinase 2 (LRRK2) modulates cytoskeletal functions by regulating actin and tubulin dynamics, thereby affecting neurite outgrowth. By interactome analysis we demonstrate that the binding of LRRK2 to tubulins is significantly enhanced by pharmacological LRRK2 inhibition in cells. Co-incubation of LRRK2 with microtubules increased the LRRK2 GTPase activity in a cell-free assay. Destabilization of microtubules causes a rapid decrease in cellular LRRK2(S935) phosphorylation indicating a decreased LRRK2 kinase activity. Moreover, both human LRRK2(G2019S) fibroblasts and mouse LRRK2(R1441G) fibroblasts exhibit alterations in cell migration in culture. Treatment of mouse fibroblasts with the selective LRRK2 inhibitor LRRK2-IN1 reduces cell motility. These findings suggest that LRRK2 and microtubules mutually interact both in non-neuronal cells and in neurons, which might contribute to our understanding of its pathogenic effects in Parkinson's disease.

journal_name

Neurobiol Dis

journal_title

Neurobiology of disease

authors

Caesar M,Zach S,Carlson CB,Brockmann K,Gasser T,Gillardon F

doi

10.1016/j.nbd.2012.12.019

subject

Has Abstract

pub_date

2013-06-01 00:00:00

pages

280-8

eissn

0969-9961

issn

1095-953X

pii

S0969-9961(13)00010-7

journal_volume

54

pub_type

杂志文章

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