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Phosphorylation of WAVE1 regulates actin polymerization and dendritic spine morphology
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Journal Article
Phosphorylation of WAVE1 regulates actin polymerization and dendritic spine morphology
2006
Overview
WAVE1—the Wiskott–Aldrich syndrome protein (WASP)-family verprolin homologous protein 1—is a key regulator of actin-dependent morphological processes
1
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.
Publisher
Nature Publishing Group UK,Nature Publishing,Nature Publishing Group
Subject
/ Animals
/ Biochemistry, Molecular Biology
/ Biological and medical sciences
/ Cyclin-Dependent Kinase 5 - metabolism
/ Fundamental and applied biological sciences. Psychology
/ Humanities and Social Sciences
/ Isolated neuron and nerve. Neuroglia
/ Kinases
/ letter
/ Male
/ Mammals
/ Mice
/ Mutants
/ Mutation
/ Neurons
/ Proteins
/ Rabbits
/ Science
