GATE-16, a membrane transport modulator, interacts with NSF and the Golgi v-SNARE GOS-28

AUTOR(ES)

Sagiv, Yuval

FONTE

Oxford University Press

RESUMO

Membrane proteins located on vesicles (v–SNAREs) and on the target membrane (t–SNAREs) mediate specific recognition and, possibly, fusion between a transport vesicle and its target membrane. The activity of SNARE molecules is regulated by several soluble cytosolic proteins. We have cloned a bovine brain cDNA encoding a conserved 117 amino acid polypeptide, denoted Golgi-associated ATPase Enhancer of 16 kDa (GATE–16), that functions as a soluble transport factor. GATE–16 interacts with N–ethylmaleimidesensitive factor (NSF) and significantly stimulates its ATPase activity. It also interacts with the Golgi v–SNARE GOS–28 in an NSF-dependent manner. We propose that GATE–16 modulates intra-Golgi transport through coupling between NSF activity and SNAREs activation.

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