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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
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
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
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
The cdc25 protein contains an intrinsic phosphatase activity
Dunphy, W. G., & Kumagai, A. (1991) · Cell · doi:10.1016/0092-8674(91)90582-j · Cited by 602
Key features of heat shock regulatory elements.
Αmin, J., Ananthan, J., & Voellmy, R. W. (1988) · Molecular and Cellular Biology · doi:10.1128/mcb.8.9.3761 · Cited by 572
Hsp90 chaperones protein folding in vitro
Wiech, H., Büchner, J., Zimmermann, R., & Jakob, U. (1992) · Nature · doi:10.1038/358169a0 · Cited by 505
Human Wee1 kinase inhibits cell division by phosphorylating p34cdc2 exclusively on Tyr15.
McGowan, C. H., & Russell, P. R. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb05633.x · Cited by 495
Self-citationHeat-shock protein hsp90 governs the activity of pp60v-src kinase.
Xu, Y., & Lindquist, S. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.15.7074 · Cited by 416
Assisting spontaneity: the role of Hsp90 and small Hsps as molecular chaperones
Jakob, U., & Büchner, J. (1994) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(94)90023-x · Cited by 381
Fission yeast genes involved in coupling mitosis to completion of DNA replication.Preprint
Enoch, T., Carr, A. M., & Nurse, P. (1992) · Genes & Development · doi:10.1101/gad.6.11.2035 · Cited by 381
p80cdc25 mitotic inducer is the tyrosine phosphatase that activates p34cdc2 kinase in fission yeast.
Millar, J. B. A., McGowan, C. H., Lenaers, G., Jones, R., & Russell, P. R. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb05008.x · Cited by 340
Self-citationRussell, P. R., & Nurse, P. (1987) · Cell · doi:10.1016/0092-8674(87)90459-4 · Cited by 331
Self-citationCutforth, T. (1994) · Cell · doi:10.1016/0092-8674(94)90442-1 · Cited by 287
p107wee1 is a dual-specificity kinase that phosphorylates p34cdc2 on tyrosine 15.
Parker, L. L., Atherton-Fessler, S., & Piwnica-Worms, H. M. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.7.2917 · Cited by 282
Dunphy, W. G. (1994) · Trends in Cell Biology · doi:10.1016/0962-8924(94)90142-2 · Cited by 276
Interaction of the Rous Sarcoma Virus Protein pp60 src with the Cellular Proteins pp50 and pp90
Brugge, J. S. (1986) · Current topics in microbiology and immunology · doi:10.1007/978-3-642-70810-7_1 · Cited by 225
cdc25+ encodes a protein phosphatase that dephosphorylates p34cdc2.
Lee, M. S., Ogg, S., Xu, M. J., Parker, L. L., Donoghue, D. J., Maller, J. L., & Piwnica-Worms, H. M. (1992) · Molecular Biology of the Cell · doi:10.1091/mbc.3.1.73 · Cited by 207
Distinct nuclear and spindle pole body populations of cyclin–cdc2 in fission yeast
Alfa, C. E., Ducommun, B., Beach, D., & Hyams, J. S. (1990) · Nature · doi:10.1038/347680a0 · Cited by 199
Key Features of Heat Shock Regulatory Elements
Αmin, J., Ananthan, J., & Voellmy, R. W. (1988) · Molecular and Cellular Biology · doi:10.1128/mcb.8.9.3761-3769.1988 · Cited by 197
Isolation of Hsp90 mutants by screening for decreased steroid receptor function.
Bohen, S. P., & Yamamoto, K. R. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.23.11424 · Cited by 195
Negative regulation of the weel protein kinase by direct action of the nim1/cdr1 mitotic inducer
Coleman, T. R. (1993) · Cell · doi:10.1016/0092-8674(93)90580-j · Cited by 185
Two distinct mechanisms for negative regulation of the Wee1 protein kinase.
Tang, Z., Coleman, T. R., & Dunphy, W. G. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb06017.x · Cited by 179
Striking conservation of TFIID in Schizosaccharomyces pombe and Saccharomyces cerevisiae
Fikes, J. D., Becker, D. M., Winston, F., & Guarente, L. (1990) · Nature · doi:10.1038/346291a0 · Cited by 166
Nim1 kinase promotes mitosis by inactivating Wee1 tyrosine kinase
Wu, L., & Russell, P. R. (1993) · Nature · doi:10.1038/363738a0 · Cited by 162
Self-citationShaknovich, R., Shue, G., & Kohtz, D. S. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.11.5059 · Cited by 154
Phosphorylation and inactivation of the mitotic inhibitor Weel by the nim1/cdr1 kinase
Parker, L. L., Walter, S. A., Young, P. G., & Piwnica-Worms, H. M. (1993) · Nature · doi:10.1038/363736a0 · Cited by 153
Thuriaux, P., Nurse, P., & Carter, B. (1978) · Molecular and General Genetics MGG · doi:10.1007/bf00274190 · Cited by 151
Carr, A. M., MacNeill, S. A., Hayles, J., & Nurse, P. (1989) · Molecular and General Genetics MGG · doi:10.1007/bf00330563 · Cited by 86
Fission yeast cyclin: subcellular localisation and cell cycle regulation
Alfa, C. E., Booher, R., Beach, D., & Hyams, J. S. (1989) · Journal of Cell Science · doi:10.1242/jcs.1989.supplement_12.2 · Cited by 45
Murray, A. W. (1993) · Current Biology · doi:10.1016/0960-9822(93)90182-n · Cited by 45
Mutational analysis of the fission yeast p34cdc2 protein kinase gene
MacNeill, S. A., & Nurse, P. (1993) · Molecular and General Genetics MGG · doi:10.1007/bf00277142 · Cited by 32
Yamazaki, M., Akogi, K., Miwa, T., Imai, T., Soeda, E., & Yokoyama, K. (1989) · Nucleic Acids Research · doi:10.1093/nar/17.17.7108 · Cited by 32
Shaknovich, R., Shue, G., & Kohtz, D. S. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.11.5059-5068.1992 · Cited by 27
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
Cited by
Sorted by citations
Hsp90 as a capacitor for morphological evolution
Rutherford, S. L., & Lindquist, S. (1998) · Nature · doi:10.1038/24550 · Cited by 2,270
Pratt, W. B., & Toft, D. O. (2003) · Experimental Biology and Medicine · doi:10.1177/153537020322800201 · Cited by 1,497
Stebbins, C. E., Russo, A. A., Schneider, C. B., Rosen, N. X., Hartl, F. U., & Pavletich, N. P. (1997) · Cell · doi:10.1016/s0092-8674(00)80203-2 · Cited by 1,370
Prodromou, C., Roe, S. M., O’Brien, R., Ladbury, J. E., Piper, P. W., & Pearl, L. H. (1997) · Cell · doi:10.1016/s0092-8674(00)80314-1 · Cited by 1,258
Role of the Heat Shock Response and Molecular Chaperones in Oncogenesis and Cell Death
Jolly, C. (2000) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/92.19.1564 · Cited by 1,052
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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
