A two-hybrid screen of the yeast proteome for Hsp90 interactors uncovers a novel Hsp90 chaperone requirement in the activity of a stress-activated mitogen-activated protein kinase, Slt2p (Mpk1p).

Millson, Stefan H.; Truman, Andrew W.; King, Victoria; Prodromou, Chrisostomos; Pearl, Laurence H.; Piper, Peter W.

doi:10.1128/ec.4.5.849-860.2005

Cited by 172Heat shock proteins researchFungal and yeast genetics researchUbiquitin and proteasome pathways

A two-hybrid screen of the yeast proteome for Hsp90 interactors uncovers a novel Hsp90 chaperone requirement in the activity of a stress-activated mitogen-activated protein kinase, Slt2p (Mpk1p).

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Millson, Stefan H., Truman, Andrew W., King, Victoria, Prodromou, Chrisostomos, Pearl, Laurence H., Piper, Peter W.·2005·Eukaryotic Cell

DOI 10.1128/ec.4.5.849-860.2005PMC PMC1140089

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Abstract

The Hsp90 chaperone cycle catalyzes the final activation step of several important eukaryotic proteins (Hsp90 "clients"). Although largely a functional form of Hsp90, an Hsp90-Gal4p DNA binding domain fusion (Hsp90-BD) displays no strong interactions in the yeast two-hybrid system, consistent with a general transience of most Hsp90-client associations. Strong in vivo interactions are though detected when the E33A mutation is introduced into this bait, a mutation that should arrest Hsp90-client complexes at a stage where the client is stabilized, yet prevented from attaining its active form. This E33A mutation stabilized the two-hybrid interactions of the Hsp90-BD fusion with approximately 3% of the Saccharomyces cerevisiae proteome in a screen of the 6,000 yeast proteins expressed as fusions to the Gal4p activation domain (AD). Among the detected interactors were the two stress-activated mitogen-activated protein (MAP) kinases of yeast, Hog1p and Slt2p (Mpk1p). Column retention experiments using wild-type and mutant forms of Hsp90 and Slt2p MAP kinase, as well as quantitative measurements of the effects of stress on the two-hybrid interaction of mutant Hsp90-BD and AD-Slt2p fusions, revealed that Hsp90 binds exclusively to the dually Thr/Tyr-phosphorylated, stress-activated form of Slt2p [(Y-P,T-P)Slt2p] and also to the MAP kinase domain within this (Y-P,T-P)Slt2p. Phenotypic analysis of a yeast mutant that expresses a mutant Hsp90 (T22Ihsp82) revealed that Hsp90 function is essential for this (Y-P,T-P)Slt2p to activate one of its downstream targets, the Rlm1p transcription factor. The interaction between Hsp90 and (Y-P,T-P)Slt2p, characterized in this study, is probably essential in this Hsp90 facilitation of the Rlm1p activation by Slt2p.

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In S. cerevisiae, Hsp90 may interact with PKC signaling by chaperoning PKC and the MAPK Slt2.
“In S. cerevisiae, Hsp90 may also interact with PKC signaling by chaperoning PKC [48] and the MAPK Slt2 [49],[50].”
From Hsp90 Governs Echinocandin Resistance in the Pathogenic Yeast Candida albicans via Calcineurin (2009) · cites this paper as [49]
The fungal Hsp90 interactome includes numerous client proteins such as receptors, protein kinases and transcription factors.
“The fungal Hsp90 interactome, which includes numerous client proteins such as receptors, protein kinases and transcription factors, displays a surprisingly high degree of plasticity that depends on environmental conditions.”
From Fungal Hsp90: a biological transistor that tunes cellular outputs to thermal inputs (2012) · cites this paper as [91]
Cell integrity signalling is down-regulated following Hsp90 depletion via destabilization of Slt2/Mkc1.
“cell integrity and Ca++-calmodulin signalling are down-regulated following Hsp90 depletion via destabilization of Slt2/Mkc191,101 and calcineurin96, respectively.”
From Fungal Hsp90: a biological transistor that tunes cellular outputs to thermal inputs (2012) · cites this paper as [91]
Conserved features of the Hsp90 interactome include a preponderance of protein kinases and transcription factors as client proteins.
“These conserved features include a preponderance of protein kinases and transcription factors as client proteins67,78,91-93.”
From Fungal Hsp90: a biological transistor that tunes cellular outputs to thermal inputs (2012) · cites this paper as [91]
Many features of the Hsp90 interactome are highly conserved from yeast to humans despite substantial network rewiring over evolutionary time.
“Also, many features of the Hsp90 interactome are highly conserved from yeast to humans despite substantial network rewiring over evolutionary time.”
From Fungal Hsp90: a biological transistor that tunes cellular outputs to thermal inputs (2012) · cites this paper as [91]

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Hsp90 and phosphorylation of the Slt2(Mpk1) MAP kinase activation loop are essential for catalytic, but not non-catalytic, Slt2-mediated transcription in yeast
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Expressed in the Yeast Saccharomyces cerevisiae , Human ERK5 Is a Client of the Hsp90 Chaperone That Complements Loss of the Slt2p (Mpk1p) Cell Integrity Stress-Activated Protein Kinase
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Investigating the protein-protein interactions of the yeast Hsp90 chaperone system by two-hybrid analysis: potential uses and limitations of this approach
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Hsp90 chaperone control over transcriptional regulation by the yeast Slt2(Mpk1)p and human ERK5 mitogen-activated protein kinases (MAPKs)
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Self-citation

Authors: Millson, S. H., Truman, A. W., King, V., Prodromou, C., Pearl, L. H., & Piper, P. W.
Affiliations: University of Sheffield (GB)
Institute of Cancer Research (GB)
Corresponding author: Piper, Peter W.
ORCID: Millson, Stefan H.
Truman, Andrew W.
Prodromou, Chrisostomos
Pearl, Laurence H.
Piper, Peter W.
Venue: Eukaryotic Cell
Publisher: American Society for Microbiology
Published: 2005-05
Volume: 4
Issue: 5
Pages: 849-860
ISSN: 1535-9778 (ISSN-L)
1535-9786
DOI: 10.1128/ec.4.5.849-860.2005
PMC: PMC1140089
OpenAlex: W2138767066
Cited by: 172
References: 75
Citations by year: 2026: 2 · 2025: 6 · 2024: 5 · 2023: 5 · 2022: 8 · 2021: 5 · 2020: 3 · 2019: 10 · 2018: 4 · 2017: 5 · 2016: 4 · 2015: 4 · 2014: 15 · 2013: 7 · 2012: 12
FWCI: 4.89
Type: journal article
Language: en
Open access: diamond
doi.org
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
Locations: Eukaryotic Cell (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Lincoln Repository (University of Lincoln) (acceptedVersion)
Figshare (submittedVersion, cc-by)
Sussex Research Online (University of Sussex) (submittedVersion)
Funders: Biotechnology and Biological Sciences Research Council (C506721/1)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Keywords: Hsp90 chaperone, Hog1p, mitogen-activated protein kinase, protein-protein interaction, Hsp90 client proteins, Saccharomyces cerevisiae, Hsp82, chaperone cycle
MeSH terms: Caffeine, Mutation, Phosphorylation, Saccharomyces cerevisiae, HSP90 Heat-Shock Proteins, Proteome, Two-Hybrid System Techniques, Mitogen-Activated Protein Kinases, Saccharomyces cerevisiae Proteins

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A two-hybrid screen of the yeast proteome for Hsp90 interactors uncovers a novel Hsp90 chaperone requirement in the activity of a stress-activated mitogen-activated protein kinase, Slt2p (Mpk1p).

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