Post-translational modifications of Hsp90 and their contributions to chaperone regulation
Open accessAbstract
Molecular chaperones, as the name suggests, are involved in folding, maintenance, intracellular transport, and degradation of proteins as well as in facilitating cell signaling. Heat shock protein 90 (Hsp90) is an essential eukaryotic molecular chaperone that carries out these processes in normal and cancer cells. Hsp90 function in vivo is coupled to its ability to hydrolyze ATP and this can be regulated by co-chaperones and post-translational modifications. In this review, we explore the varied roles of known post-translational modifications of cytosolic and nuclear Hsp90 (phosphorylation, acetylation, S-nitrosylation, oxidation and ubiquitination) in fine-tuning chaperone function in eukaryotes. This article is part of a Special Issue entitled: Heat Shock Protein 90 (HSP90).
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Multiple phosphorylation sites have been identified as regulatory elements of Hsp90 function in human and yeast.
“Multiple phosphorylation sites have been identified as regulatory elements of Hsp90 function in human and yeast (13–15).”
From Identification of a Key Lysine Residue in Heat Shock Protein 90 Required for Azole and Echinocandin Resistance in Aspergillus fumigatus (2014) · cites this paper as [13]
Activation of Hsp90 and interactions with its client proteins and cochaperones are mediated by posttranslational modifications.
“Activation of Hsp90 and interactions with its client proteins and cochaperones are mediated by posttranslational modifications, such as phosphorylation, acetylation, oxidation, S-nitrosylation, and ubiquitination (13).”
From Identification of a Key Lysine Residue in Heat Shock Protein 90 Required for Azole and Echinocandin Resistance in Aspergillus fumigatus (2014) · cites this paper as [13]
Hsp90 interacts with a large network of client proteins.
“As a chaperone, Hsp90 interacts with a large network of client proteins, and posttranslational modifications, such as phosphorylation and acetylation, are known to play important roles in its activation and in the regulation of these interactions (13).”
From Identification of a Key Lysine Residue in Heat Shock Protein 90 Required for Azole and Echinocandin Resistance in Aspergillus fumigatus (2014) · cites this paper as [13]
Phosphorylation of S49 was previously reported in human Hsp90 (corresponding human site S63).
“While phosphorylation of S49 was previously reported in human Hsp90 (corresponding human site S63) (13)”
From Identification of a Key Lysine Residue in Heat Shock Protein 90 Required for Azole and Echinocandin Resistance in Aspergillus fumigatus (2014) · cites this paper as [13]
Posttranslational modifications such as phosphorylation and acetylation play important roles in Hsp90 activation and in regulation of its interactions.
“As a chaperone, Hsp90 interacts with a large network of client proteins, and posttranslational modifications, such as phosphorylation and acetylation, are known to play important roles in its activation and in the regulation of these interactions (13).”
From Identification of a Key Lysine Residue in Heat Shock Protein 90 Required for Azole and Echinocandin Resistance in Aspergillus fumigatus (2014) · cites this paper as [13]
Internal acetylation of lysine residues has recently emerged as an important posttranslational modification of Hsp90.
“Internal acetylation of lysine residues has recently emerged as an important posttranslational modification of Hsp90 (13, 16, 21).”
From Identification of a Key Lysine Residue in Heat Shock Protein 90 Required for Azole and Echinocandin Resistance in Aspergillus fumigatus (2014) · cites this paper as [13]
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References 140 · Cited by 288
Research works printed but not linked: 1
- [34]MacLean M Picard D Cdc37 goes beyond Hsp90 and kinases Cell Stress Chaperones 8 2003 114 119 14627196 PMC514862
- Authors
- Mollapour, M., & Neckers, L.
- Affiliations
- National Institutes of Health (US)
- National Cancer Institute (US)
- Corresponding author
- Mollapour, Mehdi
- Neckers, Len
- Venue
- Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
- Publisher
- Elsevier BV
- Published
- 2012-03
- Volume
- 1823
- Issue
- 3
- Pages
- 648-655
- ISSN
- 0167-4889 (ISSN-L)
- PMC
- PMC3226900
- OpenAlex
- W2042809289
- Cited by
- 288
- References
- 140
- Citations by year
- 2026: 3 · 2025: 11 · 2024: 13 · 2023: 13 · 2022: 16 · 2021: 11 · 2020: 24 · 2019: 30 · 2018: 27 · 2017: 21 · 2016: 24 · 2015: 28 · 2014: 28 · 2013: 21 · 2012: 17
- FWCI
- 1.87
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Biochimica et Biophysica Acta (BBA) - Molecular Cell Research (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- NIH, National Cancer Institute, Center for Cancer Research
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Keywords
- HSP90, post-translational modification, molecular chaperones, phosphorylation, acetylation, S-nitrosylation, oxidation, ubiquitination, co-chaperones, ATP hydrolysis, protein folding, cancer
- MeSH terms
- Adenosine Triphosphate, Humans, Phosphorylation, Protein Processing, Post-Translational, Molecular Chaperones, HSP90 Heat-Shock Proteins
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