Desmosomal Glycoprotein DGI, a Component of Intercellular Desmosome Junctions, is Related to the Cadherin Family of Cell Adhesion Molecules

Among the variety of specialized intercellular junctions, those of the adherens type have the most obvious association with cytoskeletal elements. This may be with the actin microfilament system as in the zonula adherens or with intermediate filaments as in the macula adherens, or desmosome. In the...

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Published in:Proceedings of the National Academy of Sciences - PNAS Vol. 88; no. 11; pp. 4796 - 4800
Main Authors: Wheeler, G. N., Parker, A. E., Thomas, C. L., Ataliotis, P., Poynter, D., Arnemann, J., Rutman, A. J., Pidsley, S. C., Watt, F. M., Rees, D. A., Buxton, R. S., Magee, A. I.
Format: Journal Article
Language:English
Published: Washington, DC National Academy of Sciences of the United States of America 01-06-1991
National Acad Sciences
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Summary:Among the variety of specialized intercellular junctions, those of the adherens type have the most obvious association with cytoskeletal elements. This may be with the actin microfilament system as in the zonula adherens or with intermediate filaments as in the macula adherens, or desmosome. In the former case, it is clear that transmembrane glycoproteins of the cadherin family are important adhesive components of the molecular assembly. We now show for desmosomes that a major glycoprotein component (desmosomal glycoprotein DGI) has extensive homology with the cadherins, defining an extended family, but also has unique features in its cytoplasmic domain that are likely to be relevant to the association with intermediate rather than actin filaments. A novel 282-residue extension contains repeats of ≈29 amino acid residues predicted to have an antiparallel β-sheet structure, followed by a glycine-rich sequence. As in the cadherins, the extracellular domain contains possible Ca2+-binding sequences and a potential protease processing site. The cell adhesion recognition region (His-Ala-Val) of the cadherins is modified to Arg-Ala-Leu.
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ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.88.11.4796