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The heat shock protein 70 family: Highly homologous proteins with overlapping and distinct functions
Abstract
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.
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A gene atlas of the mouse and human protein-encoding transcriptomes
Su, A. I., Wiltshire, T., Batalov, S., Lapp, H., Ching, K. A., Block, D., Zhang, J., Soden, R., Hayakawa, M., Kreiman, G., et al. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0400782101 · Cited by 3,475
Heat Shock Protein 70 Promotes Cell Survival by Inhibiting Lysosomal Membrane Permeabilization
Nylandsted, J., Gyrd-Hansen, M., Danielewicz, A., Fehrenbacher, N., Lademann, U., Høyer-Hansen, M., Weber, E., Multhoff, G., Rohde, M., & Jäättelä, M. (2004) · The Journal of Experimental Medicine · doi:10.1084/jem.20040531 · Cited by 545
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Cited by
Enge, M., Arda, H. E., Mignardi, M., Beausang, J., Bottino, R., Kim, S. K., & Quake, S. R. (2017) · Cell · doi:10.1016/j.cell.2017.09.004 · Cited by 568
Hsp70 stabilizes lysosomes and reverts Niemann–Pick disease-associated lysosomal pathology
Kirkegaard, T., Roth, A. G., Petersen, N. H. T., Mahalka, A. K., Olsen, O. D., Moilanen, I., Zylicz, A., Knudsen, J., Sandhoff, K., Arenz, C., et al. (2010) · Nature · doi:10.1038/nature08710 · Cited by 519
Self-citationA Small Molecule Inhibitor of Inducible Heat Shock Protein 70
Leu, J. I.-J., Pimkina, J., Frank, A., Murphy, M. E., & George, D. L. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.09.023 · Cited by 441
Massey, A. J., Williamson, D. S., Browne, H., Murray, J. B., Dokurno, P., Shaw, T., Macias, A. T., Daniels, Z., Geoffroy, S., Dopson, M., et al. (2010) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s00280-009-1194-3 · Cited by 313
Dual Targeting of HSC70 and HSP72 Inhibits HSP90 Function and Induces Tumor-Specific Apoptosis
Powers, M. V., Clarke, P. A., & Workman, P. (2008) · Cancer Cell · doi:10.1016/j.ccr.2008.08.002 · Cited by 307
Metadata
- Authors
- Daugaard, M., Rohde, M., & Jäättelä, M.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2007-05-25
- Volume
- 581
- Issue
- 19
- Pages
- 3702-3710
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2043433277
- Cited by
- 1,148
- References
- 2
- FWCI
- 18.92
- Type
- journal article
- Language
- en
- Open access
- closed
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