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Coordinated Activation of Hsp70 Chaperones
Abstract
Hsp70s are a ubiquitous family of molecular chaperones involved in many cellular processes. Two Hsp70s, Lhs1p and Kar2p, are required for protein biogenesis in the yeast endoplasmic reticulum. Here, we found that Lhs1p and Kar2p specifically interacted to couple, and coordinately regulate, their respective activities. Lhs1p stimulated Kar2p by providinga specific nucleotide exchange activity, whereas Kar2p reciprocally activated the Lhs1p adenosine triphosphatase (ATPase). The two ATPase activities are coupled, and their coordinated regulation is essential for normal function in vivo.
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Citations
Cited by
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Protein Quality Control in the Cytosol and the Endoplasmic Reticulum: Brothers in Arms
Buchberger, A., Bukau, B., & Sommer, T. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.10.001 · Cited by 483
Protein Quality Control in the Endoplasmic Reticulum
Adams, B. M., Oster, M. E., & Hebert, D. N. (2019) · The Protein Journal · doi:10.1007/s10930-019-09831-w · Cited by 142
Diversity and evolution of protein translocation.
Pohlschröder, M., Hartmann, E., Hand, N. J., Dilks, K., & Haddad, A. (2005) · Annual Review of Microbiology · doi:10.1146/annurev.micro.59.030804.121353 · Cited by 122
Metadata
- Authors
- Steel, G. J., Fullerton, D. M., Tyson, J. R., & Stirling, C. J.
- Venue
- Science
- Published
- 2004-01-02
- Volume
- 303
- Issue
- 5654
- Pages
- 98-101
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2077250786
- Cited by
- 203
- References
- 0
- FWCI
- 6.12
- Type
- journal article
- Language
- en
- Open access
- closed
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