ArticleEukaryotic cell2006
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.
Article in Eukaryotic cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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47 citing papers in PubMed, 65 citations in OpenAlex.
- The transcription factor Rlm1 couples the MAPK Slt2/ERK1 pathway to the IRE1-driven unfolded protein response.Communications biology · 2026Article
- Conserved and rewired MAPK networks in human fungal pathogens.FEMS yeast research · 2026Review
- Integration of human ERKs and DUSPs into the yeast cell wall integrity pathway.Scientific reports · 2025Article
- Mechanosensor-mediated Hsp70 phosphorylation orchestrates the landscape of the heat shock response.Nature communications · 2025Article
- Coupling the MAPK Slt2/ERK1 Pathway and IRE1-driven UPR Through Transcription Factor Rlm1/MEF2.Research square · 2025Article
- ATP plays a structural role in Hsp90 function.Nature communications · 2025Article
- Review
- 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
- Identification of a Novel ERK5 (MAPK7) Inhibitor, MHJ-627, and Verification of Its Potent Anticancer Efficacy in Cervical Cancer HeLa Cells.Current issues in molecular biology · 2023Article
- Nucleotide exchange is sufficient for Hsp90 functions in vivo.Nature communications · 2023Article
- A specialized Hsp90 co-chaperone network regulates steroid hormone receptor response to ligand.Cell reports · 2022Article
- Review
- Hsp90 and phosphorylation of the Slt2(Mpk1) MAP kinase activation loop are essential for catalytic, but not non-catalytic, Slt2-mediated transcription in yeast.Cell stress & chaperones · 2022Article
- Control of Gene Expression via the Yeast CWI Pathway.International journal of molecular sciences · 2022Review
- A walk-through MAPK structure and functionality with the 30-year-old yeast MAPK Slt2.International microbiology : the official journal of the Spanish Society for Microbiology · 2021Review
- Cdk8 Kinase Module: A Mediator of Life and Death Decisions in Times of Stress.Microorganisms · 2021Review
- Hsp70-nucleotide exchange factor (NEF) Fes1 has non-NEF roles in degradation of gluconeogenic enzymes and cell wall integrity.PLoS genetics · 2019Article
- Stressing out or stressing in: intracellular pathways for SAPK activation.Current genetics · 2019Review
- Novel insights into molecular chaperone regulation of ribonucleotide reductase.Current genetics · 2019Review
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8 authors at 2 institutions in 1 country.
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Abstract
ERK5 is a mitogen-activated protein (MAP) kinase regulated in human cells by diverse mitogens and stresses but also suspected of mediating the effects of a number of oncogenes. Its expression in the slt2Delta Saccharomyces cerevisiae mutant rescued several of the phenotypes caused by the lack of Slt2p (Mpk1p) cell integrity MAP kinase. ERK5 is able to provide this cell integrity MAP kinase function in yeast, as it is activated by the cell integrity signaling cascade that normally activates Slt2p and, in its active form, able to stimulate at least one key Slt2p target (Rlm1p, the major transcriptional regulator of cell wall genes). In vitro ERK5 kinase activity was abolished by Hsp90 inhibition. ERK5 activity in vivo was also lost in a strain that expresses a mutant Hsp90 chaperone. Therefore, human ERK5 expressed in yeast is an Hsp90 client, despite the widely held belief that the protein kinases of the MAP kinase class are non-Hsp90-dependent activities. Two-hybrid and protein binding studies revealed that strong association of Hsp90 with ERK5 requires the dual phosphorylation of the TEY motif in the MAP kinase activation loop. These phosphorylations, at positions adjacent to the Hsp90-binding surface recently identified for a number of protein kinases, may cause a localized rearrangement of this MAP kinase region that leads to creation of the Hsp90-binding surface. Complementation of the slt2Delta yeast defect by ERK5 expression establishes a new tool with which to screen for novel agonists and antagonists of ERK5 signaling as well as for isolating mutant forms of ERK5.
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