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Background
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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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Background
References
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- Sou,Y.S., J. Biol. Chem. 281 (6), 3017-3024 (2006)
- Mehrle,A., Nucleic Acids Res. 34 (DATABASE ISSUE), D415-D418 (2006)
- Wiemann,S., Genome Res. 14 (10B), 2136-2144 (2004)
- Sagiv,Y., EMBO J. 19 (7), 1494-1504 (2000)
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