Septins at the annulus of mammalian sperm

Biol Chem. 2011 Aug;392(8-9):799-803. doi: 10.1515/BC.2011.074. Epub 2011 Jul 11.

Abstract

The annulus is an electron-dense ring structure connecting the midpiece and the principal piece of the mammalian sperm flagellum. Proteins from the septin family have been shown to localize to the annulus. A septin complex is assembled early in spermiogenesis with the cochaperone DNAJB13 and, in mature sperm, associates with Testis Anion Transporter 1; SLC26A8 (Tat1), a transmembrane protein of the SLC26 family. Studies in mice have shown that the annulus acts as a barrier to protein diffusion and controls correct organization of the midpiece. Consistent with these findings, absence of the annulus is associated with flagellum differentiation defects and asthenozoospermia in humans.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Anion Transport Proteins / metabolism
  • Antiporters / metabolism
  • Apoptosis Regulatory Proteins
  • Asthenozoospermia / metabolism
  • Asthenozoospermia / physiopathology
  • Heat-Shock Proteins / metabolism
  • Humans
  • Infertility, Male / metabolism
  • Infertility, Male / physiopathology
  • Male
  • Mice
  • Models, Biological
  • Molecular Chaperones
  • Protein Binding
  • Sperm Tail / metabolism*
  • Sperm Tail / physiology
  • Spermatozoa / metabolism*
  • Spermatozoa / physiology
  • Sulfate Transporters

Substances

  • Anion Transport Proteins
  • Antiporters
  • Apoptosis Regulatory Proteins
  • DNAJB13 protein, human
  • Heat-Shock Proteins
  • Molecular Chaperones
  • SLC26A8 protein, human
  • Sulfate Transporters