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The HSP70 chaperone machinery: J proteins as drivers of functional specificity
Open accessAbstract
Heat shock 70 kDa proteins (HSP70s) are ubiquitous molecular chaperones that function in a myriad of biological processes, modulating polypeptide folding, degradation and translocation across membranes, and protein–protein interactions. This multitude of roles is not easily reconciled with the universality of the activity of HSP70s in ATP-dependent client protein-binding and release cycles. Much of the functional diversity of the HSP70s is driven by a diverse class of cofactors: J proteins. Often, multiple J proteins function with a single HSP70. Some target HSP70 activity to clients at precise locations in cells and others bind client proteins directly, thereby delivering specific clients to HSP70 and directly determining their fate.
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Cites
Molecular model for a complete clathrin lattice from electron cryomicroscopy
Fotin, A., Cheng, Y., Sliz, P., Grigorieff, N., Harrison, S. C., Kirchhausen, T., & Walz, T. (2004) · Nature · doi:10.1038/nature03079 · Cited by 541
Polypeptide Flux through Bacterial Hsp70
Teter, S. A., Houry, W. A., Ang, D., Tradler, T., Rockabrand, D., Fischer, G., Blum, P., Georgopoulos, C., & Hartl, F. U. (1999) · Cell · doi:10.1016/s0092-8674(00)80787-4 · Cited by 424
Cited by
Molecular chaperones in protein folding and proteostasis
Hartl, F. U., Bracher, A., & Hayer-Hartl, M. (2011) · Nature · doi:10.1038/nature10317 · Cited by 3,381
The Biology of Proteostasis in Aging and Disease
Labbadia, J., & Morimoto, R. I. (2015) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060614-033955 · Cited by 1,472
Rosenzweig, R., Nillegoda, N. B., Mayer, M. P., & Bukau, B. (2019) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-019-0133-3 · Cited by 1,285
Verghese, J., Abrams, J., Wang, Y., & Morano, K. A. (2012) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.05018-11 · Cited by 575
A Molecular Web: Endoplasmic Reticulum Stress, Inflammation, and Oxidative Stress
Chaudhari, N., Talwar, P., Parimisetty, A., Lefebvre d’Hellencourt, C., & Ravanan, P. (2014) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2014.00213 · Cited by 600
Metadata
- Authors
- Kampinga, H. H., & Craig, E. A.
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2010-08
- Volume
- 11
- Issue
- 8
- Pages
- 579-592
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- OpenAlex
- W1972121275
- Cited by
- 1,755
- References
- 2
- FWCI
- 4.75
- Type
- journal article
- Language
- en
- Open access
- green
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