The heat shock protein 70 family: Highly homologous proteins with overlapping and distinct functions

By M. Daugaard, M. Rohde, M. Jäättelä. FEBS Letters, 2007

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The human heat shock protein 70 (Hsp70) family contains at least eight homologous chaperone proteins. Endoplasmatic reticulum and mitochondria have their specific Hsp70 proteins, whereas the remaining six family members reside mainly in the cytosol and nucleus. The requirement for multiple highly homologous although different Hsp70 proteins is still far from clear, but their individual and tissue‐specific expression suggests that they are assigned distinct biological tasks. This concept is supported by the fact that mice knockout for different Hsp70 genes display remarkably discrete phenotypes. Moreover, emerging data suggest that individual Hsp70 proteins can bring about non‐overlapping and chaperone‐independent functions essential for growth and survival of cancer cells. This review summarizes our present knowledge of the individual members of human Hsp70 family and elaborate on the functional differences between the cytosolic/nuclear representatives.

Subfields: Molecular Biology, Physical and Theoretical Chemistry

View Paper: https://www.semanticscholar.org/paper/c66e121a812cb01d9b75731884f20fc82deb07e8

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Citations in the corpus

• HSP expression in bivalves (2008, background): “, 2006); ii) an ATPase domain; iii) a peptide binding domain; iv) a G/P-rich C-terminal domain region, which enables the proteins to bind co-chaperones and other HSP (Daugaard et al., 2007), and contains intracellular localization signal sequences (Fig.”
• Lysosomal membrane permeabilization in cell death (2008, background): “Endogenous inhibitors of lysosome-mediated cell death Heat-shock (Hsp)70 proteins function as ATP-dependent chaperones that regulate the folding of newly synthesized proteins, the assembly of multiprotein complexes and the transport of proteins across cellular membranes (Daugaard et al., 2007b).”