Phosphorylation of WAVE1 regulates actin polymerization and dendritic spine morphology.

Abstract:

:WAVE1--the Wiskott-Aldrich syndrome protein (WASP)--family verprolin homologous protein 1--is a key regulator of actin-dependent morphological processes in mammals, through its ability to activate the actin-related protein (Arp2/3) complex. Here we show that WAVE1 is phosphorylated at multiple sites by cyclin-dependent kinase 5 (Cdk5) both in vitro and in intact mouse neurons. Phosphorylation of WAVE1 by Cdk5 inhibits its ability to regulate Arp2/3 complex-dependent actin polymerization. Loss of WAVE1 function in vivo or in cultured neurons results in a decrease in mature dendritic spines. Expression of a dephosphorylation-mimic mutant of WAVE1 reverses this loss of WAVE1 function in spine morphology, but expression of a phosphorylation-mimic mutant does not. Cyclic AMP (cAMP) signalling reduces phosphorylation of the Cdk5 sites in WAVE1, and increases spine density in a WAVE1-dependent manner. Our data suggest that phosphorylation/dephosphorylation of WAVE1 in neurons has an important role in the formation of the filamentous actin cytoskeleton, and thus in the regulation of dendritic spine morphology.

journal_name

Nature

journal_title

Nature

authors

Kim Y,Sung JY,Ceglia I,Lee KW,Ahn JH,Halford JM,Kim AM,Kwak SP,Park JB,Ho Ryu S,Schenck A,Bardoni B,Scott JD,Nairn AC,Greengard P

doi

10.1038/nature04976

subject

Has Abstract

pub_date

2006-08-17 00:00:00

pages

814-7

issue

7104

eissn

0028-0836

issn

1476-4687

pii

nature04976

journal_volume

442

pub_type

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