title: Molecular details of formin-mediated actin assembly.
abstract: Formins are a large family of multi-domain polypeptides that form homodimers. The highly conserved formin homology 2 (FH2) domain and its neighboring formin homology 1 (FH1) domain, which are surrounded by regulatory domains, cooperate in rapidly assembling profilin-actin into long filaments while remaining continuously associated with the fast-growing barbed end. Recent biochemical, biophysical, theoretical and structural studies have concluded that diverse formins are mechanistically similar, but that the rates of various assembly states differ quantitatively, and have shed light on the mechanism of formin auto-regulation and activation by Rho GTPases.
authors.affiliation: Department of Molecular Genetics and Cell Biology, The University of Chicago, CLSC, 920 East 58(th) Street, Chicago, Illinois 60637, USA. drkovar@uchicago.edu
authors.forename: David R
authors.initials: DR
authors.lastname: Kovar
mesh_terms: D008841:Actin Cytoskeleton / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure*; D000199:Actins / Q000737:chemistry / Q000378:metabolism*; D000818:Animals; D001704:Biopolymers / Q000737:chemistry; D002352:Carrier Proteins / Q000737:chemistry / Q000235:genetics; D003285:Contractile Proteins / Q000378:metabolism; D000080865:Formins; D008840:Microfilament Proteins / Q000737:chemistry / Q000502:physiology*; D008954:Models, Biological; D051304:Profilins / Q000737:chemistry; D017434:Protein Structure, Tertiary
chemical_list: D000199:Actins; D001704:Biopolymers; D002352:Carrier Proteins; D003285:Contractile Proteins; C491464:Diap1 protein, mouse; D000080865:Formins; D008840:Microfilament Proteins; D051304:Profilins