Abstract
The E-cadherin cell adhesion molecule is associated with cytoplasmic polypeptides, and this association is essential for its cell-binding function. Using isolated adherens junctions of the liver, we purified a 102 kd protein that can associate with E-cadherin (CAP102) and isolated cDNAs encoding this protein. Sequence analysis of the cDNAs revealed that this protein has a similarity to vinculin. L cells not expressing endogenous cadherin express the mRNA for CAP102 but have only a trace amount of CAP102 protein. Introducing exogenous E-cadherin into these cells, however, induced a high expression of CAP102 protein without affecting the amount of its mRNA, suggesting that there is a posttranscriptional regulatory mechanism for this molecule. The same effect was observed by introducing N- or P-cadherin into L cells.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Base Sequence
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Blotting, Northern
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Cadherins / genetics*
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Cadherins / isolation & purification
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Cadherins / metabolism*
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Cell Line
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Cytoskeletal Proteins / genetics*
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Cytoskeletal Proteins / isolation & purification
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Cytoskeletal Proteins / metabolism
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DNA / genetics
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DNA / isolation & purification
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Gene Expression Regulation*
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L Cells / physiology
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Mice
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Molecular Sequence Data
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Nucleic Acid Hybridization
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Organ Specificity
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RNA Processing, Post-Transcriptional*
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RNA, Messenger / genetics
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Restriction Mapping
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Sequence Homology, Nucleic Acid
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Teratoma
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Transfection
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Vinculin
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alpha Catenin
Substances
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Cadherins
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Ctnna1 protein, mouse
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Cytoskeletal Proteins
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RNA, Messenger
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alpha Catenin
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Vinculin
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DNA
Associated data
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GENBANK/D90362
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GENBANK/M60958
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GENBANK/M60959
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GENBANK/M60960
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GENBANK/M60961
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GENBANK/M60962
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GENBANK/M63447
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GENBANK/M64383
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GENBANK/M64384
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GENBANK/M86183