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Heat shock proteins: Molecules with assorted functions

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  • Published:
Frontiers in Biology

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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  1. Department of Genetics, University of Delhi, South Campus, Benito Juarez Road, New Delhi, 110021, India

    Surajit Sarkar, M. Dhruba Singh & Renu Yadav

  2. Division of Biology, MC156-29, California Institute of Technology, 1200 East California Boulevard, Pasadena, CA, 91125, USA

    Surajit Sarkar, K. P. Arunkumar & Geoffrey W. Pittman

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Sarkar, S., Singh, M.D., Yadav, R. et al. Heat shock proteins: Molecules with assorted functions. Front. Biol. 6, 312–327 (2011). https://doi.org/10.1007/s11515-011-1080-3

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