GATE-16, a Membrane Transport Modulator, Interacts with NSF and the Golgi V-SNARE GOS-28

Overview

Journal EMBO J

Specialties Biotechnology
Molecular Biology

Date 2000 Apr 4

PMID 10747018

Citations 95

Authors

Y Sagiv

A Porat

Z Elazar

Affiliations

Soon will be listed here.

Abstract

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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