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Heat shock proteins: Molecules with assorted functions |
Surajit SARKAR1,2(email.png), M. Dhruba SINGH1, Renu YADAV1, K. P. ARUNKUMAR2, Geoffrey W. PITTMAN2 |
1. 1. Department of Genetics, University of Delhi, South Campus, Benito Juarez Road, New Delhi-110021, India; 2. 2. Division of Biology, MC156-29, California Institute of Technology, 1200 East California Boulevard, Pasadena, CA 91125, USA |
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Abstract Heat shock proteins (Hsps) or molecular chaperones, are highly conserved protein families present in all studied organisms. Following cellular stress, the intracellular concentration of Hsps generally increases several folds. Hsps undergo ATP-driven conformational changes to stabilize unfolded proteins or unfold them for translocation across membranes or mark them for degradation. They are broadly classified in several families according to their molecular weights and functional properties. Extensive studies during the past few decades suggest that Hsps play a vital role in both normal cellular homeostasis and stress response. Hsps have been reported to interact with numerous substrates and are involved in many biological functions such as cellular communication, immune response, protein transport, apoptosis, cell cycle regulation, gametogenesis and aging. The present review attempts to provide a brief overview of various Hsps and summarizes their involvement in diverse biological activities.
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Keywords
heat shock protein
chaperone
chaperonin
Hsp100
Hsp90
Hsp70
Hsp60
sHsps
fertility
apoptosis
cytoskeleton
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Corresponding Author(s):
SARKAR Surajit,Email:sarkar@south.du.ac.in, sarkar@caltech.edu
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Issue Date: 01 August 2011
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