Journal
JOURNAL OF CELL SCIENCE
Volume 117, Issue 4, Pages 559-570Publisher
COMPANY OF BIOLOGISTS LTD
DOI: 10.1242/jcs.00893
Keywords
cell polarity; cell membrane; intercellular junctions; intracellular membranes; metabolism
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Funding
- NIGMS NIH HHS [R01 GM035527, GM35227] Funding Source: Medline
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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.
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