Mechanism of recruiting Sec6/8 (exocyst) complex to the apical junctional complex during polarization of epithelial cells

被引:139
作者
Yeaman, C [1 ]
Grindstaff, KK [1 ]
Nelson, WJ [1 ]
机构
[1] Stanford Univ, Sch Med, Beckman Ctr Mol & Genet Med, Dept Cellular & Mol Physiol, Stanford, CA 94305 USA
关键词
cell polarity; cell membrane; intercellular junctions; intracellular membranes; metabolism;
D O I
10.1242/jcs.00893
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Sec6/8 (exocyst) complex regulates vesicle delivery and polarized membrane growth in a variety of cells, but mechanisms regulating Sec6/8 localization are unknown. In epithelial cells, Sec6/8 complex is recruited to cell-cell contacts with a mixture of junctional proteins, but then sorts out to the apex of the lateral membrane with components of tight junction and nectin complexes. Sec6/8 complex fractionates in a high molecular mass complex with tight junction proteins and a portion of E-cadherin, and co-immunoprecipitates with cell surface-labeled E-cadherin and nectin-2alpha. Recruitment of Sec6/8 complex to cell-cell contacts can be achieved in fibroblasts when E-cadherin and nectin-2alpha are co-expressed. These results support a model in which localized recruitment of Sec6/8 complex to the plasma membrane by specific cell-cell adhesion complexes defines a site for vesicle delivery and polarized membrane growth during development of epithelial cell polarity.
引用
收藏
页码:559 / 570
页数:12
相关论文
共 67 条