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The heat shock protein 70 family: Highly homologous proteins with overlapping and distinct functions
Author(s) -
Daugaard Mads,
Rohde Mikkel,
Jäättelä Marja
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.05.039
Subject(s) - hsp70 , chaperone (clinical) , homologous chromosome , heat shock protein , cytosol , biology , phenotype , microbiology and biotechnology , protein family , mitochondrion , homologous recombination , protein superfamily , hsp90 , gene , nucleus , genetics , biochemistry , medicine , pathology , enzyme
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.