Cited by 261Heat shock proteins researchMicrotubule and mitosis dynamicsCancer-related Molecular Pathways

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A role for Hsp90 in cell cycle control: Wee1 tyrosine kinase activity requires interaction with Hsp90.

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Aligue, R., Akhavan‐Niak, H., Russell, P.·1994·The EMBO Journal

DOI 10.1002/j.1460-2075.1994.tb06956.xPMC PMC395589

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Abstract

Wee1 protein kinase regulates the length of G2 phase by carrying out the inhibitory tyrosyl phosphorylation of Cdc2-cyclin B kinase. Mutations were isolated that suppressed the G2 cell cycle arrest caused by overproduction of Wee1. One class of swo (suppressor of wee1 overproduction) mutation, exemplified by swo1-26, also caused a temperature sensitive lethal phenotype in a wee1+ background. The swo1+ gene encodes a member of the Hsp90 family of stress proteins. Swo1 is essential for viability at all temperatures. Swo1 coimmunoprecipitates with Wee1, showing that the two proteins interact. The swo1-26 mutant undergoes premature mitosis when grown at a semi-permissive temperature. These data strongly indicate that formation of active Wee1 tyrosine kinase requires interaction with Swo1, perhaps in a manner analogous to the previously demonstrated interaction between Hsp90 and v-src tyrosine kinase. These observations demonstrate a unexpected role for Hsp90 in cell cycle control.

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Authors: Aligue, R., Akhavan‐Niak, H., & Russell, P.
Affiliations: Scripps Research Institute (US)
ORCID: Russell, P.
Venue: The EMBO Journal
Publisher: Springer Science and Business Media LLC
Published: 1994-12-01
Volume: 13
Issue: 24
Pages: 6099-6106
ISSN: 0261-4189 (ISSN-L)
1460-2075
DOI: 10.1002/j.1460-2075.1994.tb06956.x
PMC: PMC395589
OpenAlex: W1509643601
Cited by: 261
References: 41
Citations by year: 2026: 1 · 2025: 3 · 2024: 3 · 2023: 3 · 2022: 4 · 2021: 3 · 2020: 3 · 2019: 5 · 2018: 9 · 2017: 4 · 2016: 7 · 2015: 3 · 2014: 6 · 2013: 7 · 2012: 4
FWCI: 5.70
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
Locations: The EMBO Journal (publishedVersion)
Europe PMC (PubMed Central) (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: Ministerio de Economía y Competitividad
National Institutes of Health
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
Keywords: HSP90, WEE1, cell cycle regulation, G2 cell cycle arrest, tyrosine kinase activity, protein-protein interaction, premature mitosis, temperature-sensitive lethality
MeSH terms: Amino Acid Sequence, Base Sequence, Cell Cycle, Enzyme Stability, Genes, Fungal, Genes, Lethal, Hot Temperature, Mitosis, Molecular Sequence Data, Mutation, Nuclear Proteins, Protein-Tyrosine Kinases, Schizosaccharomyces, Suppression, Genetic, Gene Expression Regulation, Fungal, Sequence Homology, Amino Acid, Cell Cycle Proteins, HSP90 Heat-Shock Proteins, Schizosaccharomyces pombe Proteins

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A role for Hsp90 in cell cycle control: Wee1 tyrosine kinase activity requires interaction with Hsp90.

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