Non diaphanous formin delphilin acts as a barbed end capping protein.
Formins are multi domain proteins present ubiquitously in all eukaryotes from lower fungi to higher vertebrates. Formins are characterized by the presence of formin homology domain-2 (FH2) and formin homology domain-1 (FH1). There are fifteen different formins present in mouse and human. Among these metazoan formins, Delphilin is a unique formin having two PDZ domains at the N-terminus and FH1, FH2 domain at the C-terminus respectively. In this study we observed that Delphilin binds to actin filaments, and Delphilin inhibits actin filament elongation like barbed end capping protein CapZ. In vitro, Delphilin stabilized actin filaments by inhibiting actin filament depolymerisation. Therefore, our study demonstrates Delphilin as an actin-filament capping protein.
['Dutta|Priyanka|P|', 'Das|Swagata|S|', 'Maiti|Sankar|S|']
D008841:Actin Cytoskeleton D000199:Actins D000818:Animals D051347:CapZ Actin Capping Protein D005326:Fetal Proteins D000080865:Formins D006801:Humans D051379:Mice D008840:Microfilament Proteins D009419:Nerve Tissue Proteins D009687:Nuclear Proteins D017434:Protein Structure, Tertiary
Formin Delphilin Actin and barbed end capping Expression