Evidence map›Paper›PMID 18558651›Full record

ArticleGenetics2008

Identification of Clb2 residues required for Swe1 regulation of Clb2-Cdc28 in Saccharomyces cerevisiae.

Fangfang Hu, Yan Gan, Oscar M Aparicio

Open access · bronzeAbstract read
In one paragraph

Article in Genetics, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.1field-weighted citation impact, top 27% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

13 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
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  11. The Renaissance or the cuckoo clock.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2011
    Review
  12. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Fangfang HuMolecular and Computational Biology Program, University of Southern California, Los Angeles, California 90089-2910, USA.
Yan Gan
Oscar M Aparicio
University of Southern California · US

Funding

Regulation of Chromosomal DNA Replication Dynamics in S. CerevisiaeR01GM065494 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI APARICIO, OSCAR M · 2003 to 2022
$6.9M
NIGMS NIH HHS GM-65494NIGMS NIH HHS R01 GM065494
6 · The paper itself

Abstract

Wee1 kinases regulate the cell cycle through inhibitory phosphorylation of cyclin-dependent kinases (CDKs). Eukaryotic cells express multiple CDKs, each having a kinase subunit (Cdk) and a regulatory "cyclin" subunit that function at different stages of the cell cycle to regulate distinct processes. The cyclin imparts specificity to CDK-substrate interactions and also determines whether a particular CDK is subject to Wee1 regulation. Saccharomyces Wee1 (Swe1) inhibits Cdc28 (Cdk1) associated with the mitotic cyclin, Clb2, but not with the G(1) (Cln1, -2, and -3) or the S-phase (Clb5 and -6) cyclins. Here, we show that this specificity depends on two amino acids associated with a conserved "hydrophobic patch" (HP) motif on the cyclin surface, which mediates specificity of CDK-substrate interactions. Mutation of Clb2 residues N260 and K270 largely abrogates Clb2-Cdc28 regulation by Swe1, and reciprocal mutation of the corresponding residues in Clb5 can subject Clb5-Cdc28 to regulation by Swe1. Swe1 phosphorylation by Clb2-Cdc28, which is thought to activate Swe1 kinase, depends on N260 and K270, suggesting that specific regulation of Clb2-Cdc28 by Swe1 derives from the specific ability of Clb2 to target Swe1 for activating phosphorylation. The stable association of Swe1 with Clb2-Cdc28 also depends on these residues, suggesting that Swe1 may competitively inhibit Clb2-Cdc28 interactions with substrates, in addition to its well-known function as a regulator of CDK activity through tyrosine phosphorylation.

Indexed as

Amino Acid SequenceCDC28 Protein Kinase, S cerevisiaeCell CycleCell Cycle ProteinsCyclin BGenes, FungalHydrophobic and Hydrophilic InteractionsMolecular Sequence DataMultiprotein ComplexesPhosphorylationProtein SubunitsProtein-Tyrosine KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidSubstrate SpecificityCDC28 Protein Kinase, S cerevisiaeCell Cycle ProteinsCLB2 protein, S cerevisiaeCyclin BMultiprotein ComplexesProtein SubunitsProtein-Tyrosine KinasesSaccharomyces cerevisiae ProteinsSWE1 protein, S cerevisiaeTyrosine

Identifiers

PMID18558651
PMCPMC2429880
OpenAlexW1979377474

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.