ArticleMolecular biology of the cell1998
Hsp90 is required for pheromone signaling in yeast.
Article in Molecular biology of the cell, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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Who cites it
56 citing papers in PubMed, 112 citations in OpenAlex.
- Saccharomyces cerevisiae as a tool for deciphering Hsp90 molecular chaperone function.Essays in biochemistry · 2023Article
- Activation of autophagy depends on Atg1/Ulk1-mediated phosphorylation and inhibition of the Hsp90 chaperone machinery.Cell reports · 2023Article
- Article
- Ydj1 interaction at nucleotide-binding-domain of yeast Ssa1 impacts Hsp90 collaboration and client maturation.PLoS genetics · 2022Article
- Comprehensive characterization of the Hsp70 interactome reveals novel client proteins and interactions mediated by posttranslational modifications.PLoS biology · 2022Article
- Heat shock proteins and the calcineurin-crz1 signaling regulate stress responses in fungi.Archives of microbiology · 2022Review
- The Role of Stress Proteins in Haloarchaea and Their Adaptive Response to Environmental Shifts.Biomolecules · 2020Review
- CgSTE11 mediates cross tolerance to multiple environmental stressors in Candida glabrata.Scientific reports · 2019Article
- Post-translational Regulation of FNIP1 Creates a Rheostat for the Molecular Chaperone Hsp90.Cell reports · 2019Article
- Evidence for interaction between Hsp90 and the ER membrane complex.Cell stress & chaperones · 2018Article
- Preferences in a trait decision determined by transcription factor variants.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- A Chemogenomic Screening Platform Used to Identify Chemotypes Perturbing HSP90 Pathways.SLAS discovery : advancing life sciences R & D · 2017Article
- ir-HSP: Improved Recognition of Heat Shock Proteins, Their Families and Sub-types Based OnFrontiers in genetics · 2017Article
- Hsp90 Maintains Proteostasis of the Galactose Utilization Pathway To Prevent Cell Lethality.Molecular and cellular biology · 2016Article
- Systematic Mutant Analyses Elucidate General and Client-Specific Aspects of Hsp90 Function.Cell reports · 2016Article
- Mps1 Mediated Phosphorylation of Hsp90 Confers Renal Cell Carcinoma Sensitivity and Selectivity to Hsp90 Inhibitors.Cell reports · 2016Article
- PredHSP: Sequence Based Proteome-Wide Heat Shock Protein Prediction and Classification Tool to Unlock the Stress Biology.PloS one · 2016Article
- c-Abl Mediated Tyrosine Phosphorylation of Aha1 Activates Its Co-chaperone Function in Cancer Cells.Cell reports · 2015Article
- Both the charged linker region and ATPase domain of Hsp90 are essential for Rad51-dependent DNA repair.Eukaryotic cell · 2015Article
- Role of Heat-Shock Proteins in Cellular Function and in the Biology of Fungi.Biotechnology research international · 2015Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The heat-shock protein 90 (Hsp90) is a cytosolic molecular chaperone that is highly abundant even at normal temperature. Specific functions for Hsp90 have been proposed based on the characterization of its interactions with certain transcription factors and kinases including Raf in vertebrates and flies. We therefore decided to address the role of Hsp90 for MAP kinase pathways in the budding yeast, an organism amenable to both genetic and biochemical analyses. We found that both basal and induced activities of the pheromone-signaling pathway depend on Hsp90. Signaling is defective in strains expressing low levels or point mutants of yeast Hsp90 (Hsp82), or human Hsp90beta instead of the wild-type protein. Ste11, a yeast equivalent of Raf, forms complexes with wild-type Hsp90 and depends on Hsp90 function for accumulation. For budding yeast, Ste11 represents the first identified endogenous "substrate" of Hsp90. Moreover, Hsp90 functions in steroid receptor and pheromone signaling can be genetically separated as the Hsp82 point mutant T525I and the human Hsp90beta are specifically defective for the former and the latter, respectively. These findings further corroborate the view that molecular chaperones must also be considered as transient or stable components of signal transduction pathways.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.