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SNARE anchorage

Membrane fusion is driven by formation of complexes involving SNARE proteins supplied by each bilayer. SNARES such as SNAP-25 are palmitoylated at cysteine residues, which allows their insertion into the plasma membrane. Whether this is essential for fusion or simply targets them to the right place is unclear, however, since soluble SNAP-25 mutants can drive membrane fusion in vitro but cannot support exocytosis in some permeabilized cell models. Giulia Baldini and co-workers have approached this problem in an `intact cell' system, stably transfecting neuroblastoma cells with Botulinum neurotoxin E (a protein that cleaves endogenous SNAP25) and examining the ability of toxin-insensitive forms of SNAP25 to drive exocytosis (see p. 3341). The authors find that a mutant lacking the cysteine-rich domain that contains the palmitoylation sequence cannot drive exocytosis in intact cells, nor can it form SNARE complexes when present at normal levels. Significantly, Baldini and co-workers find that the mutant can form complexes when overexpressed. They therefore propose that palmitoylation of SNAP-25 serves to concentrate it locally in the membrane to levels sufficient for exocytosis.

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Related articles in JCS:

Plasma membrane targeting of SNAP-25 increases its local concentration and is necessary for SNARE complex formation and regulated exocytosis

Darshan K. Koticha, Ellen E. McCarthy, and Giulia Baldini
JCS 2002 115: 3341-3351. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content Social Bookmarking                         What's this?