SNAP FAMILY OF NSF ATTACHMENT PROTEINS INCLUDES A BRAIN-SPECIFIC ISOFORM

被引：237

作者：

WHITEHEART, SW

GRIFF, IC

BRUNNER, M

CLARY, DO

MAYER, T

BUHROW, SA

ROTHMAN, JE

机构：

[1] Rockefeller Research Laboratory, Memorial Sloan-Kettering Cancer Center, New York, NY 10021

[2] Institut für Physiologische Chemie, Universtät München, D-8000 München

[3] HHMI University of California San Francisco, San Francisco

来源：

NATURE | 1993年 / 362卷 / 6418期

关键词：

D O I：

10.1038/362353a0

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

THE soluble NSF attachment proteins (SNAPs) enable N-ethyl-maleimide-sensitive fusion protein (NSF) to bind to target membranes1-3. Here we report the cloning and sequencing of complementary DNAs encoding alpha-, beta- and gamma-SNAPs. Two of these proteins, alpha and gamma, are found in a wide range of tissues, and act synergistically in intra-Golgi transport. The third, beta, is a brain-specific isoform of alpha-SNAP. Thus, NSF and SNAPs appear to be general components of the intracellular membrane fusion apparatus, and their action at specific sites of fusion must be controlled by SNAP receptors particular to the membranes being fused, as described in the accompanying article4.

引用

页码：353 / 355

页数：3

共 14 条

[11]

SZTUL E, 1993, J BIOL CHEM, V268, P1876

[12] BINDING OF AN N-ETHYLMALEIMIDE SENSITIVE FUSION PROTEIN TO GOLGI MEMBRANES REQUIRES BOTH A SOLUBLE PROTEIN(S) AND AN INTEGRAL MEMBRANE-RECEPTOR [J].