|
mDia1 (also known as Dia1, Drf1 for Diaphanous-related formin-1, Diaph1, KIAA4062, p140mDia, mKIAA4062, D18Wsu154e) is a protein. It is the mouse version of the diaphanous homolog 1 of Drosophila. It belongs to the protein family called the formins and is a Rho effector. It localizes to the mitotic spindle and midbody, plays a role in stress fiber and filopodia formation, phagocytosis, activation of serum response factor, a transcription factor, and formation of adherens junction. mDia1 accelerates actin nucleation and elongation by interacting with barbed ends (fast-growing ends) of actin filaments. The gene encoding mDia1 is located on Chromosome 18 of Mus musculus and named ''Diap1''. mDia1 is highly homologous to Drosophila diaphanous, regulating the cytokinetic ring during cytokinesis.〔 Homologues in other species are known as well, like the human DIAP1, budding yeast's Bni1 or Cdc12p of ''S. pombe''. The gene has been knocked-out in mice. == Structure == The product of the ''Diap1'' (''Diaph1'') gene consists of 1255 amino acids resulting in a molecular weight of 139,343 Da. The mDia1 polypeptide chain can be divided into four regions: * GBD/FH3 (Rho GTPase-binding domain/formin homology 3)domain (366 amino acids long): positions 75-440 * FH1 (formin homology 1) domain (162 amino acids long): positions 586-747 * FH2 (formin homology 2) domain (403 amino acids long): positions 752-1154 * DAD (diaphanous autoregulatory domain) (29 amino acids long): positions 1177-1205 Three supplementary domains were discovered: * coiled coil (103 amino acids long): positions 460-562 * coiled coil (153 amino acids long): positions 1027-1179 * Arg/Lys-rich domain (4 amino acids long): positions: 1196-1199 The active region of the C terminus consists of formin homology 1 and 2 (FH1 and FH2) and the Dia autoregulatory domain (DAD). The FH1 domain is predicted to be rope-like and it contains binding sites for profilin-actin complexes. The adjacent FH2 domain forms together with the FH2 domain of a second mDia1 molecule a head-to-tail doughnut shaped dimer that encircles the barbed end of an actin filament. Thus the FH2 domain has the ability to dimerize.〔 The N terminus consists of a Rho GTPase-binding domain (GBD), which is joint to the formin homology 3 (FH3). DAD can mediate autoinhibition through interactions with the Dia inhibitory domain (DID), which is a subdomain of the GDB/FH3 domain (see section Regulation). 抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』 ■ウィキペディアで「MDia1」の詳細全文を読む スポンサード リンク
|