Formin proteins: a domain-based approach.
Formin proteins are potent regulators of actin dynamics. Most eukaryotes have multiple formin isoforms, suggesting diverse cellular roles. Formins are modular proteins, containing a series of domains and functional motifs. The Formin homology 2 (FH2) domain binds actin filament barbed ends and moves processively as these barbed ends elongate or depolymerize. The FH1 domain influences FH2 domain function through binding to the actin monomer-binding protein, profilin. Outside of FH1 and FH2, amino acid similarity between formins decreases, suggesting diverse mechanisms for regulation and cellular localization. Some formins are regulated by auto-inhibition through interaction between the diaphanous inhibitory domain (DID) and diaphanous auto-regulatory domain (DAD), and activated by Rho GTPase binding to GTPase-binding domains (GBD). Other formins lack DAD, DID and GBD, and their regulatory mechanisms await elucidation.
Higgs
Henry N
HN
Department of Biochemistry, Dartmouth Medical School, Hanover NH 03755, USA. henry.higgs@dartmouth.edu
D000199:Actins / Q000378:metabolism*; D000818:Animals; D002352:Carrier Proteins / Q000378:metabolism; D003285:Contractile Proteins / Q000378:metabolism*; D005326:Fetal Proteins; D000080865:Formins; D006801:Humans; D008840:Microfilament Proteins / Q000737:chemistry / Q000378:metabolism*; D008958:Models, Molecular; D009687:Nuclear Proteins; D051304:Profilins; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D020741:rho GTP-Binding Proteins / Q000378:metabolism
D000199:Actins; D002352:Carrier Proteins; D003285:Contractile Proteins; C491462:DIAPH2 protein, human; C491464:Diap1 protein, mouse; D005326:Fetal Proteins; D000080865:Formins; D008840:Microfilament Proteins; D009687:Nuclear Proteins; C495738:PFN1 protein, human; D051304:Profilins; D020741:rho GTP-Binding Proteins