A Role for a 70-Kilodalton Heat Shock Protein in Lysosomal Degradation of Intracellular Proteins

Hui-Ling Chiang(Tufts University), Stanley R. Terlecky(Tufts University), Charles P. Plant(Tufts University), J. Fred Dice(Tufts University)
Science
October 20, 1989
Cited by 966

Abstract

A 73-kilodalton (kD) intracellular protein was found to bind to peptide regions that target intracellular proteins for lysosomal degradation in response to serum withdrawal. This protein cross-reacted with a monoclonal antibody raised to a member of the 70-kD heat shock protein (hsp70) family, and sequences of two internal peptides of the 73-kD protein confirm that it is a member of this family. In response to serum withdrawal, the intracellular concentration of the 73-kD protein increased severalfold. In the presence of adenosine 5′-triphosphate (ATP) and MgCl 2 , the 73-kD protein enhanced protein degradation in two different cell-free assays for lysosomal proteolysis.


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