The di-leucine motif of vesicle-associated membrane protein 4 is required for its localization and AP-1 binding
The di-leucine motif of vesicle-associated membrane protein 4 is required for its localization and AP-1 binding
复制标题
DOI：
10.1074/jbc.m106646200
复制
发表时间：
2001-12-28
影响因子：
4.8
通讯作者：
Scheller, RH
中科院分区：
文献类型：
--
作者：
Peden, AA;Park, GY;Scheller, RH
异四聚体接头复合体和圈套在膜出芽和融合的特异性中起着关键作用。在这里，我们检验了囊泡萌发和膜融合是通过这些分子的相互作用而耦合的假设。我们研究了囊泡相关膜蛋白4(VAMP4)的二亮氨酸基序在VAMP4的接头结合和定位中的作用。二亮氨酸基序的突变在体外抑制AP-1的结合，并影响VAMP4在体内的稳态分布。
Heterotetrameric adaptor complexes and SNAREs play key roles in the specificity of membrane budding and fusion. Here we test the hypothesis that vesicle budding and membrane fusion are coupled by the interaction of these molecules. We investigate the role of the di-leucine motif of vesicle-associated membrane protein 4 (VAMP4) in adaptor binding and localization of VAMP4. Mutation of the di-leucine motif inhibits AP-1 binding in vitro and affects the steady state distribution of VAMP4 in vivo.