title: Spatiotemporal regulation of the Pak1 kinase.
abstract: Pak1 (p21-activated kinase 1) is a key regulator of the actin cytoskeleton, adhesion and cell motility. Such biological roles require a tight spatial and kinetic control of its localization and activity. We summarize here the current knowledge on Pak1 dynamics in vivo. Inactive dimeric Pak1 is mainly cytosolic. Localized interaction with the activators Cdc42-GTP and Rac1-GTP stimulates the kinase at the sites of cellular protrusions. Moreover, Pak1 is dynamically engaged into multiprotein complexes forming adhesions to the extracellular matrix. Cutting edge microscopy technologies on living cells are finally shedding light on the intricate spatiotemporal mechanisms regulating Pak1.
authors.affiliation: INSERM U528, Institut Curie, Section de Recherche, 26 rue d'Ulm, 75005 Paris, France. parrini@curie.fr
authors.forename: M C
authors.initials: MC
authors.lastname: Parrini
authors.forename: M
authors.initials: M
authors.lastname: Matsuda
authors.forename: J
authors.initials: J
authors.lastname: de Gunzburg
mesh_terms: D000818:Animals; D020134:Catalytic Domain; D002465:Cell Movement; D019281:Dimerization; D011487:Protein Conformation; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry* / Q000378:metabolism*; D054462:p21-Activated Kinases
chemical_list: D017346:Protein Serine-Threonine Kinases; D054462:p21-Activated Kinases