| Autor: |
Yeaman, Charles, Grindstaff, Kent K., Nelson, W. James |
| Předmět: |
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| Zdroj: |
Journal of Cell Science; 2/1/2004, Vol. 117 Issue 4, p559-570, 12p, 13 Color Photographs, 30 Black and White Photographs, 9 Graphs |
| Abstrakt: |
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 Ecadherin and nectin-2α. Recruitment of Sec6/8 complex to cell-cell contacts can be achieved in fibroblasts when Ecadherin and nectin-2α 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. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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