ArticleThe Journal of cell biology1997
The yeast CDC37 gene interacts with MPS1 and is required for proper execution of spindle pole body duplication.
Article in The Journal of cell biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 59 citations in OpenAlex.
- Comparative analysis of the impact of Heat shock protein 90 kDa or Cdc37 mutation on the yeast proteome.Cell stress & chaperones · 2026Article
- Insights into Hsp90 mechanism andFrontiers in molecular biosciences · 2024Review
- Impact of Co-chaperones and Posttranslational Modifications Toward Hsp90 Drug Sensitivity.Sub-cellular biochemistry · 2023Article
- Mps1 Mediated Phosphorylation of Hsp90 Confers Renal Cell Carcinoma Sensitivity and Selectivity to Hsp90 Inhibitors.Cell reports · 2016Article
- Novel interaction between the co-chaperone Cdc37 and Rho GTPase exchange factor Vav3 promotes androgen receptor activity and prostate cancer growth.The Journal of biological chemistry · 2013Article
- Centrosome duplication proceeds during mimosine-induced G1 cell cycle arrest.Journal of cellular physiology · 2008Article
- Alteration of the protein kinase binding domain enhances function of the Saccharomyces cerevisiae molecular chaperone Cdc37.Eukaryotic cell · 2007Article
- The Schizosaccharomyces pombe Cdc7 protein kinase required for septum formation is a client protein of Cdc37.Eukaryotic cell · 2007Article
- Mechanisms regulating the protein kinases of Saccharomyces cerevisiae.Eukaryotic cell · 2007Review
- Cdc37p is required for stress-induced high-osmolarity glycerol and protein kinase C mitogen-activated protein kinase pathway functionality by interaction with Hog1p and Slt2p (Mpk1p).Eukaryotic cell · 2007Article
- Cdc37 has distinct roles in protein kinase quality control that protect nascent chains from degradation and promote posttranslational maturation.The Journal of cell biology · 2007Article
- Discovery of biological networks from diverse functional genomic data.Genome biology · 2005Article
- Cdc37 goes beyond Hsp90 and kinases.Cell stress & chaperones · 2003Review
- Cdc37 is essential for chromosome segregation and cytokinesis in higher eukaryotes.The EMBO journal · 2002Article
- Polo-like kinases and centrosome regulation.Oncogene · 2002Review
- Centrosomes and checkpoints: the MPS1 family of kinases.Oncogene · 2002Review
- The yeast protein kinase Mps1p is required for assembly of the integral spindle pole body component Spc42p.The Journal of cell biology · 2002Article
- A mammalian homolog of yeast MOB1 is both a member and a putative substrate of striatin family-protein phosphatase 2A complexes.The Journal of biological chemistry · 2001Article
- p50(Cdc37) can buffer the temperature-sensitive properties of a mutant of Hck.Molecular and cellular biology · 2000Article
- Cdc37 promotes the stability of protein kinases Cdc28 and Cak1.Molecular and cellular biology · 2000Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The MPS1 gene from Saccharomyces cerevisiae encodes an essential protein kinase required for spindle pole body (SPB) duplication and for the mitotic spindle assembly checkpoint. Cells with the mps1-1 mutation fail early in SPB duplication and proceed through monopolar mitosis with lethal consequences. We identified CDC37 as a multicopy suppressor of mps1-1 temperature-sensitive growth. Suppression is allele specific, and synthetic lethal interactions occur between mps1 and cdc37 alleles. We examined the cdc37-1 phenotype for defects related to the SPB cycle. The cdc37-1 temperature-sensitive allele causes unbudded, G1 arrest at Start (Reed, S.I. 1980. Genetics. 95: 561-577). Reciprocal shifts demonstrate that cdc37-1 arrest is interdependent with alpha-factor arrest but is not a normal Start arrest. Although the cells are responsive to alpha-factor at the arrest, SPB duplication is uncoupled from other aspects of G1 progression and proceeds past the satellite-bearing SPB stage normally seen at Start. Electron microscopy reveals side-by-side SPBs at cdc37-1 arrest. The outer plaque of one SPB is missing or reduced, while the other is normal. Using the mps2-1 mutation to distinguish between the SPBs, we find that the outer plaque defect is specific to the new SPB. This phenotype may arise in part from reduced Mps1p function: although Mps1p protein levels are unaffected by the cdc37-1 mutation, kinase activity is markedly reduced. These data demonstrate a requirement for CDC37 in SPB duplication and suggest a role for this gene in G1 control. CDC37 may provide a chaperone function that promotes the activity of protein kinases.
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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.