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GATE‐16, a membrane transport modulator, interacts with NSF and the Golgi v‐SNARE GOS‐28
Author(s) -
Sagiv Yuval,
LegesseMiller Aster,
Porat Amir,
Elazar Zvulun
Publication year - 2000
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/19.7.1494
Subject(s) - biology , golgi apparatus , microbiology and biotechnology , vesicular transport protein , vesicle , vesicular transport proteins , transport protein , fusion protein , vesicle fusion , lipid bilayer fusion , membrane protein , biochemistry , synaptic vesicle , membrane , endoplasmic reticulum , cytoplasm , gene , recombinant dna , vacuole , vacuolar protein sorting
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 G olgi‐associated AT Pase E nhancer 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.