i-SNAREs: inhibitory SNAREs that fine-tune the specificity of membrane fusion

J Cell Biol. 2004 Jan 5;164(1):79-88. doi: 10.1083/jcb.200307066. Epub 2003 Dec 29.

Abstract

A new functional class of SNAREs, designated inhibitory SNAREs (i-SNAREs), is described here. An i-SNARE inhibits fusion by substituting for or binding to a subunit of a fusogenic SNAREpin to form a nonfusogenic complex. Golgi-localized SNAREs were tested for i-SNARE activity by adding them as a fifth SNARE together with four other SNAREs that mediate Golgi fusion reactions. A striking pattern emerges in which certain subunits of the cis-Golgi SNAREpin function as i-SNAREs that inhibit fusion mediated by the trans-Golgi SNAREpin, and vice versa. Although the opposing distributions of the cis- and trans-Golgi SNAREs themselves could provide for a countercurrent fusion pattern in the Golgi stack, the gradients involved would be strongly sharpened by the complementary countercurrent distributions of the i-SNAREs.

Publication types

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

MeSH terms

  • Binding Sites / physiology
  • Golgi Apparatus / metabolism*
  • Golgi Apparatus / ultrastructure
  • Intracellular Membranes / chemistry
  • Intracellular Membranes / metabolism*
  • Intracellular Membranes / ultrastructure
  • Membrane Fusion / physiology*
  • Membrane Proteins / classification
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism*
  • Protein Binding / physiology
  • Protein Subunits / metabolism
  • Protein Transport / physiology
  • SNARE Proteins
  • Signal Transduction / physiology
  • Vesicular Transport Proteins*
  • trans-Golgi Network / physiology

Substances

  • Membrane Proteins
  • Protein Subunits
  • SNARE Proteins
  • Vesicular Transport Proteins