Document Detail


The tyrosine kinase substrate p120cas binds directly to E-cadherin but not to the adenomatous polyposis coli protein or alpha-catenin.
MedLine Citation:
PMID:  7651399     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The tyrosine kinase substrate p120cas (CAS), which is structurally similar to the cell adhesion proteins beta-catenin and plakoglobin, was recently shown to associate with the E-cadherin-catenin cell adhesion complex. beta-catenin, plakoglobin, and CAS all have an Arm domain that consists of 10 to 13 repeats of a 42-amino-acid motif originally described in the Drosophila Armadillo protein. To determine if the association of CAS with the cadherin cell adhesion machinery is similar to that of beta-catenin and plakoglobin, we examined the CAS-cadherin-catenin interactions in a number of cell lines and in the yeast two-hybrid system. In the prostate carcinoma cell line PC3, CAS associated normally with cadherin complexes despite the specific absence of alpha-catenin in these cells. However, in the colon carcinoma cell line SW480, which has negligible E-cadherin expression, CAS did not associate with beta-catenin, plakoglobin, or alpha-catenin, suggesting that E-cadherin is the protein which bridges CAS to the rest of the complex. In addition, CAS did not associate with the adenomatous polyposis coli (APC) tumor suppressor protein in any of the cell lines analyzed. Interestingly, expression of the various CAS isoforms was quite heterogeneous in these tumor cell lines, and in the colon carcinoma cell line HCT116, which expresses normal levels of E-cadherin and the catenins, the CAS1 isoforms were completely absent. By using the yeast two-hybrid system, we confirmed the direct interaction between CAS and E-cadherin and determined that CAS Arm repeats 1 to 10 are necessary and sufficient for this interaction. Hence, like beta-catenin and plakoglobin, CAS interacts directly with E-cadherin in vivo; however, unlike beta-catenin and plakoglobin, CAS does not interact with APC or alpha-catenin.
Authors:
J M Daniel; A B Reynolds
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Molecular and cellular biology     Volume:  15     ISSN:  0270-7306     ISO Abbreviation:  Mol. Cell. Biol.     Publication Date:  1995 Sep 
Date Detail:
Created Date:  1995-09-22     Completed Date:  1995-09-22     Revised Date:  2010-01-29    
Medline Journal Info:
Nlm Unique ID:  8109087     Medline TA:  Mol Cell Biol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  4819-24     Citation Subset:  IM    
Affiliation:
Department of Tumor Cell Biology, St. Jude Children's Research Hospital, Memphis, Tennessee 38105, USA.
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MeSH Terms
Descriptor/Qualifier:
Adenomatous Polyposis Coli Protein
Cadherins / metabolism*
Cell Adhesion Molecules / metabolism*
Colonic Neoplasms
Cytoskeletal Proteins / metabolism*
Humans
Male
Phosphoproteins / metabolism*
Prostatic Neoplasms
Protein Binding
Recombinant Proteins / metabolism
Tumor Cells, Cultured
Yeasts / genetics
alpha Catenin
Grant Support
ID/Acronym/Agency:
CA55724/CA/NCI NIH HHS; P30 CA21756/CA/NCI NIH HHS
Chemical
Reg. No./Substance:
0/Adenomatous Polyposis Coli Protein; 0/CTNNA1 protein, human; 0/Cadherins; 0/Cell Adhesion Molecules; 0/Cytoskeletal Proteins; 0/Phosphoproteins; 0/Recombinant Proteins; 0/alpha Catenin; 0/delta catenin
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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