A thioredoxin fold protein Sh3bgr regulates Enah and is necessary for proper sarcomere formation

Dev Biol. 2015 Sep 1;405(1):1-9. doi: 10.1016/j.ydbio.2015.06.005. Epub 2015 Jun 24.

Abstract

The sh3bgr (SH3 domain binding glutamate-rich) gene encodes a small protein containing a thioredoxin-like fold, SH3 binding domain, and glutamate-rich domain. Originally, it was suggested that increased expression of Sh3bgr may cause the cardiac phenotypes in Down's syndrome. However, it was recently reported that the overexpression of Sh3bgr did not cause any disease phenotypes in mice. In this study, we have discovered that Sh3bgr is critical for sarcomere formation in striated muscle tissues and also for heart development. Sh3bgr is strongly expressed in the developing somites and heart in Xenopus. Morpholino mediated-knockdown of sh3bgr caused severe malformation of heart tissue and disrupted segmentation of the somites. Further analysis revealed that Sh3bgr specifically localized to the Z-line in mature sarcomeres and that knockdown of Sh3bgr completely disrupted sarcomere formation in the somites. Moreover, overexpression of Sh3bgr resulted in abnormally discontinues thick firmaments in the somitic sarcomeres. We suggest that Sh3bgr does its function at least partly by regulating localization of Enah for the sarcomere formation. In addition, we provide the data supporting Sh3bgr is also necessary for proper heart development in part by affecting the Enah protein level.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Embryo, Nonmammalian / metabolism
  • Female
  • Gene Knockdown Techniques
  • Humans
  • Microfilament Proteins / chemistry*
  • Microfilament Proteins / metabolism*
  • Muscle Development
  • Muscle, Striated / embryology
  • Muscle, Striated / metabolism
  • Myocardium / metabolism
  • Protein Structure, Secondary
  • Protein Transport
  • Sarcomeres / metabolism*
  • Somites / embryology
  • Somites / metabolism
  • Thioredoxins / chemistry*
  • Thioredoxins / metabolism
  • Xenopus / embryology
  • Xenopus Proteins / chemistry*
  • Xenopus Proteins / metabolism*

Substances

  • Enah protein, Xenopus
  • Microfilament Proteins
  • Sh3bgr protein, Xenopus
  • Xenopus Proteins
  • Thioredoxins