TY - JOUR
T1 - Colocalization of calcium-dependent protease II and one of its substrates at sites of cell adhesion
AU - Beckerle, Mary C.
AU - Burridge, Keith
AU - DeMartino, George N.
AU - Croall, Dorothy E.
N1 - Funding Information:
We are particularly grateful to Maurine Vaughan for patience and skill in typing this manuscript. This research was supported by grants from the National Institutes of Health (NIH) to K. Burridge (GM 29860) and from the Texas Affiliate of the American Heart Association and the American Cancer Society (IN-142) to D. E. Croall. Support is also acknowledged from the National Science Foundation (DCB 8602131) and American Heart Association to M. C. Beckerle, and from the NIH (AM 29829) to G. N. DeMartino.
PY - 1987/11/20
Y1 - 1987/11/20
N2 - 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 α-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.
AB - 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 α-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.
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U2 - 10.1016/0092-8674(87)90126-7
DO - 10.1016/0092-8674(87)90126-7
M3 - Article
C2 - 2824061
AN - SCOPUS:0023661249
SN - 0092-8674
VL - 51
SP - 569
EP - 577
JO - Cell
JF - Cell
IS - 4
ER -