Phosphorylation of Wave1 Regulates Actin Polymerization and Dendritic Spine Morphology.
From: Laboratory of Molecular and Cellular Neuroscience, The Rockefeller University, 1230 York Avenue, New York, New York 10021, USA.
Nature
- Publish Date: Aug 2006
- ISSN: 1476-4687
- Volume: 442
- Issue: 7104
- Pages: 814-7
- Medium: Internet
- Language: English
- Citation (JAMA): Kim Yong, Sung Jee Young, Ceglia Ilaria, et al. Phosphorylation of Wave1 Regulates Actin Polymerization and Dendritic Spine Morphology.. Nature Aug 2006;442:814-7
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.
Mesh Headings (Keywords): Actins, Animals, Biopolymers, Cells, Cultured, Cyclic AMP, Cyclin-Dependent Kinase 5, Cytoskeleton, Dendrites, Male, Mice, Mice, Inbred C57BL, Phosphorylation, Rabbits, Wiskott-Aldrich Syndrome Protein Family
Check for Full Text / PubMed Unique Identifier (PMID): 16862120
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