DESMOSOMAL GLYCOPROTEIN DGI, A COMPONENT OF INTERCELLULAR DESMOSOME JUNCTIONS, IS RELATED TO THE CADHERIN FAMILY OF CELL-ADHESION MOLECULES

作者：WHEELER GN; PARKER AE; THOMAS CL; ATALIOTIS P; POYNTER D; ARNEMANN J; RUTMAN AJ; PIDSLEY SC; WATT FM; REES DA; BUXTON RS; MAGEE AI

来源：Proceedings of the National Academy of Sciences of the United States of America, 1991, 88(11): 4796-4800.

DOI：10.1073/pnas.88.11.4796

• DESMOSOME
• DESMOGLEIN
• CELL CELL JUNCTION

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 almost-equal-to 29 amino acid residues predicted to have an antiparallel beta-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.

• 出版日期1991-6
• 单位河北医科大学