The DOI matches its Crossref record; 40 of the 41 references it cites were found in a registry or an index.
A role for Hsp90 in cell cycle control: Wee1 tyrosine kinase activity requires interaction with Hsp90.
Open accessAbstract
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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In the citing paper
“Several key cell cycle regulators have been identified as Hsp90 interactors in S. cerevisiae, including Swe1, Cdc28, Cdc50 and Cdc6061,92,123.”
From Fungal Hsp90: a biological transistor that tunes cellular outputs to thermal inputs (2012) · cites this paper as [123]
In the citing paper
“Hsp90 also has evolutionarily conserved roles in cell cycle progression.”
From Fungal Hsp90: a biological transistor that tunes cellular outputs to thermal inputs (2012) · cites this paper as [123]
In the citing paper
“Hsp90's role in cell cycle progression appears to be conserved in the fungal kingdom. In the budding yeast Saccharomyces cerevisiae, Hsp90 is required for cell cycle progression during environmental stress, and in the fission yeast Schizosaccharomyces pombe Hsp90 interacts with cell cycle machinery (Aligue et al., 1994; Munoz and Jimenez, 1999; McClellan et al., 2007).”
From Cdc28 provides a molecular link between Hsp90, morphogenesis, and cell cycle progression in Candida albicans (2012) · cites this paper as Aligue et al., 1994
In the citing paper
“Several key regulators of cell cycle progression have been implicated as Hsp90 interactors, including the mammalian tyrosine kinase Wee1 and its budding yeast homologue Swe1, the polo-like kinase Plk1 and its yeast homologue Cdc5, and the cyclin-dependent kinase Cdc2 and its budding yeast homologue Cdc28 (Aligue et al., 1994; Munoz and Jimenez, 1999; de Carcer et al., 2001; Goes and Martin, 2001;”
From Cdc28 provides a molecular link between Hsp90, morphogenesis, and cell cycle progression in Candida albicans (2012) · cites this paper as Aligue et al., 1994
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Cites
Lindquist, S., & Craig, E. A. (1988) · Annual Review of Genetics · doi:10.1146/annurev.ge.22.120188.003215 · Cited by 5,304
[56] Molecular genetic analysis of fission yeast Schizosaccharomyces pombe
Moreno, S., Klar, A., & Nurse, P. (1991) · Methods in Enzymology · doi:10.1016/0076-6879(91)94059-l · Cited by 3,620
Universal control mechanism regulating onset of M-phase
Nurse, P. (1990) · Nature · doi:10.1038/344503a0 · Cited by 2,798
Tyrosine phosphorylation of the fission yeast cdc2+ protein kinase regulates entry into mitosis
Gould, K. L., & Nurse, P. (1989) · Nature · doi:10.1038/342039a0 · Cited by 1,235
Negative regulation of mitosis by wee1+, a gene encoding a protein kinase homolog
Russell, P. R., & Nurse, P. (1987) · Cell · doi:10.1016/0092-8674(87)90458-2 · Cited by 1,027
Self-citationThiamine-repressible expression vectors pREP and pRIP for fission yeast
Maundrell, K. (1993) · Gene · doi:10.1016/0378-1119(93)90551-d · Cited by 1,009
cdc25+ functions as an inducer in the mitotic control of fission yeast
Russell, P. R., & Nurse, P. (1986) · Cell · doi:10.1016/0092-8674(86)90546-5 · Cited by 982
Self-citationGenetic control of cell size at cell division in yeast
Nurse, P. (1975) · Nature · doi:10.1038/256547a0 · Cited by 868
mik1 and wee1 cooperate in the inhibitory tyrosine phosphorylation of cdc2
Lundgren, K., Walworth, N. C., Booher, R., Dembski, M., Kirschner, M. W., & Beach, D. (1991) · Cell · doi:10.1016/0092-8674(91)90266-2 · Cited by 683
Borkovich, K. A., Farrelly, F. W., Finkelstein, D. B., Taulien, J., & Lindquist, S. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.9.3919 · Cited by 641
Research works printed but not linked: 3
- Bohen,S.P. and Yamamoto,K.R. (1993) Proc. Natl Acad. Sci. USA, 90, 11424-11428.
- Parker,L.L., Atherton-Fessler,S. and Piwnica-Worms,H. (1992) Proc. Natl Acad. Sci. USA, 89, 2917-2921.
- Xu,Y. and Lindquist,S. (1993) Proc. NatI. Acad. Sci. USA, 90, 7074-7078. Received on September 7, 1994; revised on October 13, 1994
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Oun, R. R. S. (2016) · Bangor University Research Portal (Bangor University)
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Prince, T. L. (2005) · SHAREOK (University of Oklahoma; Oklahoma State University; Central Oklahoma University)
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Metadata
- Authors
- Aligue, R., Akhavan‐Niak, H., & Russell, P.
- Affiliations
- Scripps Research Institute (US)
- ORCID
- Russell, P.
- Venue
- The EMBO Journal
- Published
- 1994-12-01
- Volume
- 13
- Issue
- 24
- Pages
- 6099-6106
- ISSN
- 0261-4189 (ISSN-L)
- 1460-2075
- 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
- 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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