Molecular details of formin-mediated actin assembly

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 r...

Full description

Saved in:
Bibliographic Details
Published in:Current opinion in cell biology 2006-02, Vol.18 (1), p.11-17
Main Author: Kovar, David R
Format: Article
Language:English
Subjects:
Actin Cytoskeleton - chemistry
Actin Cytoskeleton - metabolism
Actin Cytoskeleton - ultrastructure
Actins - chemistry
Actins - metabolism
Animals
Biopolymers - chemistry
Carrier Proteins - chemistry
Carrier Proteins - genetics
Contractile Proteins - metabolism
Microfilament Proteins - chemistry
Microfilament Proteins - physiology
Models, Biological
Profilins - chemistry
Protein Structure, Tertiary
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.
ISSN:0955-0674
1879-0410
DOI:10.1016/j.ceb.2005.12.011