Frontiers in Biology

, 6:312

Heat shock proteins: Molecules with assorted functions

  • Surajit Sarkar
  • M. Dhruba Singh
  • Renu Yadav
  • K. P. Arunkumar
  • Geoffrey W. Pittman
Review

DOI: 10.1007/s11515-011-1080-3

Cite this article as:
Sarkar, S., Singh, M.D., Yadav, R. et al. Front. Biol. (2011) 6: 312. doi:10.1007/s11515-011-1080-3
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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.

Keywords

heat shock protein chaperone chaperonin Hsp100 Hsp90 Hsp70 Hsp60 sHsps fertility apoptosis cytoskeleton 

Copyright information

© Higher Education Press and Springer-Verlag Berlin Heidelberg 2011

Authors and Affiliations

  • Surajit Sarkar
    • 1
    • 2
  • M. Dhruba Singh
    • 1
  • Renu Yadav
    • 1
  • K. P. Arunkumar
    • 2
  • Geoffrey W. Pittman
    • 2
  1. 1.Department of GeneticsUniversity of DelhiNew DelhiIndia
  2. 2.Division of Biology, MC156-29California Institute of TechnologyPasadenaUSA

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