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PMID: 8236461 Published · ppublish English Journal Article Review

From cadherins to catenins: cytoplasmic protein interactions and regulation of cell adhesion.

Trends in genetics : TIG ·Vol. 9 ·No. 9 ·1993-09-00 ·Pages 317-21

Kemler R

Abstract

Classical cadherins are complexed via their cytoplasmic domains with alpha-, beta- and gamma-catenin. This complex formation links cadherins to the actin filament network and to other transmembrane and cytoplasmic proteins. alpha-Catenin is homologous to vinculin, and beta-catenin to the product of the Drosophila gene armadillo, while gamma-catenin seems to be identical to plakoglobin. Catenins are part of a higher order protein structure that is of crucial importance for the adhesive function of cadherins. A working model of the construction and regulation of this multiprotein interaction is proposed.

MeSH Terms
Actins/metabolism Animals Cadherins/chemistry,physiology Cell Adhesion/physiology Cell Adhesion Molecules/chemistry,physiology Cytoplasm/metabolism Cytoskeletal Proteins/chemistry,physiology Desmoplakins Drosophila melanogaster/genetics Humans Mice Models, Biological Trans-Activators alpha Catenin beta Catenin gamma Catenin
Chemicals
Actins CTNNA1 protein, human CTNNB1 protein, human CTNNB1 protein, mouse Cadherins Cell Adhesion Molecules Ctnna1 protein, mouse Cytoskeletal Proteins Desmoplakins JUP protein, human Jup protein, mouse Trans-Activators alpha Catenin beta Catenin gamma Catenin
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Kemler R
Max Planck Institut für Immunbiologie, Freiburg, Germany.
Article Info
Journal
Trends in genetics : TIG
Abbr.
Trends Genet
ISSN
0168-9525
Published
1993-09-00
Pages
317-21
Language
English
Region
England
NLM ID
8507085
Subset
IM
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