title: WHAMMing into the Golgi.
abstract: A new paper from Campellone et al. in a recent issue of Cell identifies WHAMM, a multifunctional protein that stimulates Arp2/3-mediated actin polymerization, binds and organizes microtubules, and influences the structure and efficiency of the Golgi complex. WHAMM's membrane localization at the entry face of the Golgi complex is novel for an actin nucleation-promoting factor, and highlights the importance of the cytoskeleton in organizing the secretory pathway.
authors.affiliation: Department of Biochemistry, Stanford University School of Medicine, Stanford, CA 94305-5307, USA.
authors.forename: Garret L
authors.initials: GL
authors.lastname: Hayes
authors.forename: Suzanne R
authors.initials: SR
authors.lastname: Pfeffer
mesh_terms: D051376:Actin-Related Protein 2-3 Complex / Q000378:metabolism; D000199:Actins / Q000378:metabolism*; D000818:Animals; D006056:Golgi Apparatus / Q000378:metabolism*; D008870:Microtubules / Q000378:metabolism*; D011506:Proteins / Q000378:metabolism*
chemical_list: D051376:Actin-Related Protein 2-3 Complex; D000199:Actins; D011506:Proteins