Evidence map›Paper›PMID 40341598›Full record

ArticleNature communications2025

Phosphate-binding pocket on cyclin B governs CDK substrate phosphorylation and mitotic timing.

Henry Y Ng, Devon H Whelpley, Armin N Adly, Robert A Maxwell, David O Morgan

Abstract read
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors.

Henry Y NgDepartment of Physiology, University of California San Francisco, San Francisco, CA, USA.ORCID http://orcid.org/0000-0002-6724-9607
Devon H WhelpleyDepartment of Physiology, University of California San Francisco, San Francisco, CA, USA.
Armin N AdlyDepartment of Physiology, University of California San Francisco, San Francisco, CA, USA.
Robert A MaxwellThe Vincent J. Coates Proteomics/Mass Spectrometry Core Laboratory, University of California, Berkeley, CA, USA.
David O MorganDepartment of Physiology, University of California San Francisco, San Francisco, CA, USA. David.morgan@ucsf.edu.ORCID http://orcid.org/0000-0001-8753-4416

Funding

Regulatory Enzymes and Systems in Cell Cycle ControlR35GM118053 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI DAVID Owen MORGAN · 2016 to 2026
$10.3M
Wide field-of-view Spinning Disk Confocal with Photoactivation and PhotobleachingS10OD017993 · OD · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI THORN, KURT · 2015 to 2015
$274k
NIGMS NIH HHS R35 GM118053NIH HHS S10 OD017993U.S. Department of Health & Human Services | NIH | National Institute of General Medical Sciences (NIGMS) R35-GM118053
6 · The paper itself

Abstract

Cell cycle progression is governed by complexes of the cyclin-dependent kinases (CDKs) and their regulatory subunits cyclin and Cks1. CDKs phosphorylate hundreds of substrates, often at multiple sites. Multisite phosphorylation depends on Cks1, which binds initial priming phosphorylation sites to promote secondary phosphorylation at other sites. Here, we describe a similar role for a recently discovered phosphate-binding pocket (PP) on B-type cyclins. Mutation of the PP in Clb2, the major mitotic cyclin of budding yeast, alters bud morphology and delays the onset of anaphase. Mutation of the PP reduces multi-site phosphorylation of CDK substrates in vitro, including the Cdc16 and Cdc27 subunits of the anaphase-promoting complex/cyclosome and the Bud6 and Spa2 subunits of the polarisome. We conclude that the cyclin PP, like Cks1, controls the pattern of multisite phosphorylation on CDK substrates, thereby helping to establish the robust timing of cell-cycle events.

Indexed as

Cyclin BCyclin-Dependent KinasesMitosisPhosphatesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsBinding SitesCell Cycle ProteinsMutationPhosphorylationSubstrate SpecificityCell Cycle ProteinsCLB2 protein, S cerevisiaeCyclin BCyclin-Dependent KinasesPhosphatesSaccharomyces cerevisiae Proteins

Identifiers

PMID40341598
PMCPMC12062237

What OpenQuestion holds

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Registered trials

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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.