The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
Hsp90-Dependent Activation of Protein Kinases Is Regulated by Chaperone-Targeted Dephosphorylation of Cdc37
Open accessAbstract
Activation of protein kinase clients by the Hsp90 system is mediated by the cochaperone protein Cdc37. Cdc37 requires phosphorylation at Ser13, but little is known about the regulation of this essential posttranslational modification. We show that Ser13 of uncomplexed Cdc37 is phosphorylated in vivo, as well as in binary complex with a kinase (C-K), or in ternary complex with Hsp90 and kinase (H-C-K). Whereas pSer13-Cdc37 in the H-C-K complex is resistant to nonspecific phosphatases, it is efficiently dephosphorylated by the chaperone-targeted protein phosphatase 5 (PP5/Ppt1), which does not affect isolated Cdc37. We show that Cdc37 and PP5/Ppt1 associate in Hsp90 complexes in yeast and in human tumor cells, and that PP5/Ppt1 regulates phosphorylation of Ser13-Cdc37 in vivo, directly affecting activation of protein kinase clients by Hsp90-Cdc37. These data reveal a cyclic regulatory mechanism for Cdc37, in which its constitutive phosphorylation is reversed by targeted dephosphorylation in Hsp90 complexes.
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Citations
Cites
Structure of TPR Domain–Peptide Complexes
Scheufler, C., Brinker, A., Bourenkov, G., Pegoraro, S., Moroder, L., Bartunik, H., Hartl, F. U., & Moarefi, I. (2000) · Cell · doi:10.1016/s0092-8674(00)80830-2 · Cited by 1,188
Crystal structure of an Hsp90–nucleotide–p23/Sba1 closed chaperone complex
Ali, M. M. U., Roe, S. M., Vaughan, C. K., Meyer, P., Panaretou, B., Piper, P. W., Prodromou, C., & Pearl, L. H. (2006) · Nature · doi:10.1038/nature04716 · Cited by 962 · cited 3×
“…an adaptor, and in common with Hsp90 cochaperones, such as Sti1, Aha1, and p23 (Prodromou et al., 1999; Panaretou et al., 2002; Meyer et al., 2004; Ali et al., 2006), Cdc37 has a regulatory function, and can arrest the ATPase-coupled chaperone cycle by preventing ATP-dependent N-terminal…”
BackgroundSelf-citationMutational Analysis of Hsp90 Function: Interactions with a Steroid Receptor and a Protein Kinase
Nathan, D. F., & Lindquist, S. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.7.3917 · Cited by 423 · cited 3×
“For agar growth GA sensitivity assays, overnight DO cultures (without methionine) were diluted to an optical density of 600 nm of 0.5, and z5 ml aliquots of a 10-fold dilution series were spotted onto DO-2% agar (without methionine) plates supplemented with the indicated level of GA. Growth was monitored over 3–5 days…”
BackgroundMethodInfluentialHeat-shock protein hsp90 governs the activity of pp60v-src kinase.
Xu, Y., & Lindquist, S. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.15.7074 · Cited by 416 · cited 2×
“The tyrosine kinase v-Src is a well-known Hsp90-Cdc37dependent client (Brugge, 1986; Xu and Lindquist, 1993), the activity of which in yeast is a widely used reporter for analysis of functionality in the Hsp90 chaperone system (Nathan and Lindquist, 1995; Panaretou et al.”
BackgroundMethodRussell, L. C., Whitt, S. R., Chen, M.-S., & Chinkers, M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.29.20060 · Cited by 165 · cited 1×
“However, this signal was not lost on overexpression of a Ppt1 mutant with mutations (K81E/R85E), known to abrogate TPR domain interaction with the C terminus of Hsp90 (Russell et al., 1999; Scheufler et al., 2000).”
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Cited by
HSP90 at the hub of protein homeostasis: emerging mechanistic insights
Taipale, M., Jarosz, D. F., & Lindquist, S. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2918 · Cited by 1,818
Schopf, F. H., Biebl, M. M., & Buchner, J. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.20 · Cited by 1,540
The Hsp90 chaperone machinery: Conformational dynamics and regulation by co-chaperones
Li, J., Soroka, J., & Buchner, J. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.09.003 · Cited by 498
Atomic structure of Hsp90-Cdc37-Cdk4 reveals that Hsp90 traps and stabilizes an unfolded kinase
Verba, K. A., Wang, R. Y.-R., Arakawa, A., Liu, Y., Shirouzu, M., Yokoyama, S., & Agard, D. A. (2016) · Science · doi:10.1126/science.aaf5023 · Cited by 424
Post-translational modifications of Hsp90 and their contributions to chaperone regulation
Mollapour, M., & Neckers, L. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.07.018 · Cited by 288
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Metadata
- Authors
- Vaughan, C. K., Mollapour, M., Smith, J. R., Truman, A., Hu, B., Good, V. M., Panaretou, B., Neckers, L., Clarke, P. A., Workman, P., Piper, P. W., Prodromou, C., & Pearl, L. H.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2008-09
- Volume
- 31
- Issue
- 6
- Pages
- 886-895
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2055304293
- Cited by
- 200
- References
- 5
- FWCI
- 4.47
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Vaughan, C. K., Mollapour, M., Smith, J. R., Truman, A., Hu, B., Good, V. M., Panaretou, B., Neckers, L., Clarke, P. A., Workman, P., Piper, P. W., Prodromou, C., & Pearl, L. H. (2008). Hsp90-Dependent Activation of Protein Kinases Is Regulated by Chaperone-Targeted Dephosphorylation of Cdc37. Molecular Cell. https://doi.org/10.1016/j.molcel.2008.07.021
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