Barfly: sculpting membranes at the Drosophila neuromuscular junction

Dev Neurobiol. 2012 Jan;72(1):33-56. doi: 10.1002/dneu.20923.

Abstract

The ability of a cell to change the shape of its membranes is intrinsic to many cellular functions. Proteins that can alter or recognize curved membrane structures and those that can act to recruit other proteins which stabilize the membrane curvature are likely to be essential in cell functions. The BAR (Bin, amphiphysin, RVS167 homology) domain is a protein domain that can either induce lipidic membranes to curve or can sense curved membranes. BAR domains are found in several proteins at neuronal synapses. We will review BAR domain structure and the role that BAR domain containing proteins play in regulating the morphology and function of the Drosophila neuromuscular junction. In flies the BAR domain containing proteins, endophilin and syndapin affect synaptic vesicle endocytosis, whereas CIP4, dRich, nervous wreck and syndapin affect synaptic morphology. We will review the growing evidence implicating mutations in BAR domain containing proteins being the cause of human pathologies.

Publication types

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

MeSH terms

  • Animals
  • Drosophila / anatomy & histology*
  • Drosophila Proteins / metabolism*
  • Endocytosis
  • Forkhead Transcription Factors / metabolism
  • Microfilament Proteins / metabolism
  • Nerve Tissue Proteins / metabolism
  • Neuromuscular Junction / cytology*
  • Neuromuscular Junction / metabolism*
  • Protein Structure, Tertiary
  • Saccharomyces cerevisiae Proteins / metabolism

Substances

  • Drosophila Proteins
  • Forkhead Transcription Factors
  • Microfilament Proteins
  • Nerve Tissue Proteins
  • RVS167 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins
  • bin protein, Drosophila
  • amphiphysin