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      Non diaphanous formin delphilin acts as a barbed end capping protein.

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          Abstract

          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.

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          Author and article information

          Journal
          Exp. Cell Res.
          Experimental cell research
          Elsevier BV
          1090-2422
          0014-4827
          May 17 2017
          Affiliations
          [1 ] Department of Biological Sciences, Indian Institute of Science Education and Research, Kolkata, India; Department of Biology, Indian Institute of Science Education and Research, Pune, India.
          [2 ] Department of Biological Sciences, Indian Institute of Science Education and Research, Kolkata, India.
          [3 ] Department of Biological Sciences, Indian Institute of Science Education and Research, Kolkata, India. Electronic address: spm@iiserkol.ac.in.
          Article
          S0014-4827(17)30276-8
          10.1016/j.yexcr.2017.05.014
          28527698
          c4671634-8cce-4f2d-b0a3-d7b371b0b788
          History

          Actin and barbed end capping,Delphilin,Expression,Formin

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