Evidence map›Paper›PMID 21135117›Full record

ArticleMolecular and cellular biology2011

Mitotic exit control of the Saccharomyces cerevisiae Ndr/LATS kinase Cbk1 regulates daughter cell separation after cytokinesis.

Jennifer Brace, Jonathan Hsu, Eric L Weiss

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

35 citing papers in PubMed, 58 citations in OpenAlex.

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  10. Hog1 activation delays mitotic exit via phosphorylation of Net1.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  11. The Multiple Roles of the Cdc14 Phosphatase in Cell Cycle Control.International journal of molecular sciences · 2020
    Review
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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.

Jennifer BraceDepartment of Molecular Biosciences, Northwestern University, Evanston, IL 60208, USA.
Jonathan Hsu
Eric L Weiss
Northwestern University · US

Funding

Control and function of the yeast RAM networkR01GM084223 · NIGMS · NORTHWESTERN UNIVERSITY · PI WEISS, ERIC LYLE · 2008 to 2017
$2.9M
Cell cycle regulation of a novel pathway directing events in late mitosisF32GM082011 · NIGMS · NORTHWESTERN UNIVERSITY · PI BRACE, JENNIFER LYNN · 2007 to 2009
$148k
NIGMS NIH HHS 5F32GM082011-03NIGMS NIH HHS 5R01GM084223-02NIGMS NIH HHS F32 GM082011NIGMS NIH HHS R01 GM084223
6 · The paper itself

Abstract

Saccharomyces cerevisiae cell division ends with destruction of a septum deposited during cytokinesis; this must occur only after the structure's construction is complete. Genes involved in septum destruction are induced by the transcription factor Ace2, which is activated by the kinase Cbk1, an Ndr/LATS-related protein that functions in a system related to metazoan hippo pathways. Phosphorylation of a conserved hydrophobic motif (HM) site regulates Cbk1; at peak levels in late mitosis we found that approximately 3% of Cbk1 carries this modification. HM site phosphorylation prior to mitotic exit occurs in response to activation of the FEAR (Cdc fourteen early anaphase release) pathway. However, HM site phosphorylation is not sufficient for Cbk1 to act on Ace2: the kinase is also negatively regulated prior to cytokinesis, likely by cyclin-dependent kinase (CDK) phosphorylation. Cbk1 cannot phosphorylate Ace2 until after mitotic exit network (MEN)-initiated release of the phosphatase Cdc14. Treatment of Cbk1 with Cdc14 in vitro does not increase its intrinsic enzymatic activity, but Cdc14 is required for Cbk1 function in vivo. Thus, we propose that Cdc14 coordinates cell separation with mitotic exit via FEAR-initiated phosphorylation of the Cbk1 HM site and MEN-activated reversal of mitotic CDK phosphorylations that block both Cbk1 and Ace2 function.

Indexed as

Amino Acid SubstitutionBase SequenceBinding SitesCell DivisionCytokinesisDNA-Binding ProteinsDNA PrimersGenes, FungalHydrophobic and Hydrophilic InteractionsIntracellular Signaling Peptides and ProteinsMitosisModels, BiologicalMutagenesis, Site-DirectedPhosphorylationProtein Serine-Threonine KinasesRecombinant Fusion ProteinsACE2 protein, S cerevisiaeCBK1 protein, S cerevisiaeDNA-Binding ProteinsDNA PrimersIntracellular Signaling Peptides and ProteinsProtein Serine-Threonine KinasesRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsTranscription Factors

Identifiers

PMID21135117
PMCPMC3028648
OpenAlexW2130652636

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.