Colocalization of calcium-dependent protease II and one of its substrates at sites of cell adhesion

Cell. 1987 Nov 20;51(4):569-77. doi: 10.1016/0092-8674(87)90126-7.

Abstract

Adhesion plaques, specialized regions of the plasma membrane where a cell contacts its substratum, are dynamic structures. However, little is known about how the protein-protein interactions that occur at adhesion plaques are controlled. One mechanism by which a cell might modulate its associations with the substratum is by selective, regulated proteolysis of an adhesion plaque component. Here we show that the catalytic subunit of the calcium-dependent protease type II (CDP-II) is localized in adhesion plaques of several cell types (BS-C-1, EBTr, and MDBK). We have compared the susceptibility of the adhesion plaque constituents vinculin, talin, and alpha-actinin to calcium-dependent proteolysis in vitro and have found talin to be the preferred substrate for CDP-II. The colocalization of a calcium-requiring proteolytic enzyme and talin in adhesion plaques raises the possibility that calcium-dependent proteolytic activity provides a mechanism for regulating some aspect of adhesion plaque physiology and function via cleavage of talin.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Actinin / metabolism
  • Animals
  • Antigens, Surface / metabolism
  • Calpain / analysis*
  • Cattle
  • Cell Adhesion Molecules
  • Cell Adhesion*
  • Cell Line
  • Chlorocebus aethiops
  • Cytoskeletal Proteins / metabolism*
  • Kidney / cytology
  • Muscle Proteins / metabolism
  • Talin
  • Vinculin

Substances

  • Antigens, Surface
  • Cell Adhesion Molecules
  • Cytoskeletal Proteins
  • Muscle Proteins
  • Talin
  • Actinin
  • Vinculin
  • Calpain