Article
The hydrophobic cysteine-rich domain of SNAP25 couples with downstream residues to mediate membrane interactions and recognition by DHHC palmitoyl transferases.
Molecular biology of the cell - 1 Mar 2009
Greaves Jennifer, Prescott Gerald R, Fukata Yuko, Fukata Masaki, Salaun Christine, Chamberlain Luke H
Abstract excerpt
SNAP25 is synthesized as a soluble protein but must associate with the plasma membrane to function in exocytosis; however, this membrane-targeting pathway is poorly defined. SNAP25 contains a palmitoylated cysteine-rich domain with four cysteines, and we show that coexpression of specific DHHC palmitoyl transferases is sufficient to promote SNAP25 membrane association in HEK293 cells. siRNA-mediated knockdown of...
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