Abstract
The Sec6/8 complex is essential for specific exocytic sites on the plasma membrane and contributes to membrane growth in mammalian cells. In Madin-Darby canine kidney (MDCK) cells, E-cadherin and nectin-based adhesion complexes recruit the Sec6/8 complex to intercellular contacts. However, in cancer cells, the relationship between the Sec6/8 complex and the cell-cell adhesion proteins remains obscure. We demonstrate that the expression of α-E-catenin is increased by Sec6 siRNAs, and E-cadherin and β-catenin localize mainly at the cell-cell contact region in HSC3 cells, which were transfected with Sec6 siRNA.
Copyright © 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
MeSH terms
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Animals
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Cadherins / genetics
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Cadherins / metabolism
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Carcinoma, Squamous Cell / genetics
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Carcinoma, Squamous Cell / metabolism*
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Carcinoma, Squamous Cell / pathology
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Cell Adhesion / physiology*
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Cell Adhesion Molecules / metabolism
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Cell Line, Tumor
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Humans
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Mouth Neoplasms / genetics
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Mouth Neoplasms / metabolism*
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Mouth Neoplasms / pathology
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Nectins
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RNA, Small Interfering / genetics
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RNA, Small Interfering / metabolism*
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Vesicular Transport Proteins / genetics
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Vesicular Transport Proteins / metabolism*
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alpha Catenin / genetics
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alpha Catenin / metabolism*
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beta Catenin / genetics
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beta Catenin / metabolism
Substances
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Cadherins
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Cell Adhesion Molecules
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EXOC3 protein, human
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Nectins
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RNA, Small Interfering
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Vesicular Transport Proteins
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alpha Catenin
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beta Catenin