Non diaphanous formin delphilin acts as a barbed end capping protein

Exp Cell Res. 2017 Aug 15;357(2):163-169. doi: 10.1016/j.yexcr.2017.05.014. Epub 2017 May 17.

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.

Keywords: Actin and barbed end capping; Delphilin; Expression; Formin.

MeSH terms

  • Actin Cytoskeleton / metabolism*
  • Actins / metabolism*
  • Animals
  • CapZ Actin Capping Protein / metabolism
  • Fetal Proteins / metabolism*
  • Formins
  • Humans
  • Mice
  • Microfilament Proteins / metabolism*
  • Nerve Tissue Proteins / metabolism*
  • Nuclear Proteins / metabolism*
  • Protein Structure, Tertiary

Substances

  • Actins
  • CAPZA1 protein, human
  • CapZ Actin Capping Protein
  • Capza1 protein, mouse
  • Fetal Proteins
  • Formins
  • Microfilament Proteins
  • Nerve Tissue Proteins
  • Nuclear Proteins
  • delphilin