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MBC in Press, published online ahead of print March 23, 2005
Mol. Biol. Cell 10.1091/mbc.E04-10-0914

A more recent version of this article appeared on June 1, 2005
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Submitted on October 21, 2004
Revised on March 2, 2005
Accepted on March 15, 2005

The PCH Family Member MAYP/PSTPIP2 Directly Regulates F-Actin Bundling and Enhances Filopodia Formation and Motility in Macrophages

Violeta Chitu,* Fiona J. Pixley,* Frank Macaluso,{dagger}{ddagger} Daniel R. Larson,{dagger} John Condeelis,{dagger}{ddagger} Yee-Guide Yeung,* and E. Richard Stanley*

Departments of *Developmental and Molecular Biology and {dagger}Anatomy and Structural Biology; and {ddagger}Analytical Imaging Facility, Albert Einstein College of Medicine, Bronx, NY 10461

Monitoring Editor: David Drubin

Macrophage Actin-Associated Tyrosine Phosphorylated Protein (MAYP) belongs to the Pombe Cdc15 Homology (PCH) family of proteins involved in the regulation of actin-based functions including cell adhesion and motility. In mouse macrophages, MAYP is tyrosine phosphorylated following activation of the colony stimulating factor-1 receptor (CSF-1R), which also induces actin reorganization, membrane ruffling, cell spreading, polarization and migration. Because MAYP associates with F-actin, we investigated the function of MAYP in regulating actin organization in macrophages. Overexpression of MAYP decreased CSF-1-induced membrane ruffling and increased filopodia formation, motility and CSF-1-mediated chemotaxis. The opposite phenotype was observed with reduced expression of MAYP, indicating that MAYP is a negative regulator of CSF-1-induced membrane ruffling and positively regulates formation of filopodia and directional migration. Overexpression of MAYP led to a reduction in total macrophage F-actin content but was associated with increased actin bundling. Consistent with this, purified MAYP bundled F-actin and regulated its turnover in vitro. In addition, MAYP colocalized with cortical and filopodial F-actin in vivo. Because filopodia are postulated to increase directional motility by acting as environmental sensors, the MAYP-stimulated increase in directional movement may be at least partly explained by enhancement of filopodia formation.

Address correspondence to: E. Richard Stanley (rstanley{at}aecom.yu.edu)




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