Evidence map›Paper›PMID 23297348›Full record

ArticleMolecular & cellular proteomics : MCP2013

Comprehensive proteomics analysis reveals new substrates and regulators of the fission yeast clp1/cdc14 phosphatase.

Jun-Song Chen, Matthew R Broadus, Janel R McLean, Anna Feoktistova, Liping Ren, Kathleen L Gould

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

36 citing papers in PubMed, 55 citations in OpenAlex.

  1. ThemicroPublication biology · 2025
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  16. Fission yeast Opy1 is an endogenous PI(4,5)PJournal of cell science · 2020
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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

6 authors at 2 institutions in 1 country.

Jun-Song ChenHoward Hughes Medical Institute and Department of Cell and Developmental Biology, Vanderbilt University School of Medicine, 1161 21 Avenue South, MCN B2309, Nashville, Tennessee 37232, USA.
Matthew R Broadus
Janel R McLean
Anna Feoktistova
Liping Ren
Kathleen L Gould
Vanderbilt University · USHoward Hughes Medical Institute · US

Funding

BIOCHEMICAL &CHEMICAL TRAINING FOR CANCER RESEARCHT32CA009582 · NCI · VANDERBILT UNIVERSITY · PI David K Cortez · 1987 to 2026
$8.8M
Integrated Biological Systems Training in OncologyT32CA119925 · NCI · VANDERBILT UNIVERSITY · PI Vivian Gama, William Patrick Tansey · 2008 to 2026
$7.6M
Howard Hughes Medical InstituteNCI NIH HHS NCI T32CA119925NCI NIH HHS N.I.H. T32 CA009582NCI NIH HHS T32 CA009582NCI NIH HHS T32 CA119925
6 · The paper itself

Abstract

The conserved family of Cdc14 phosphatases targets cyclin-dependent kinase substrates in yeast, mediating late mitotic signaling events. To discover substrates and regulators of the Schizosaccharomyces pombe Cdc14 phosphatase Clp1, TAP-tagged Clp1, and a substrate trapping mutant (Clp1-C286S) were purified from asynchronous and mitotic (prometaphase and anaphase) cells and binding partners were identified by 2D-LC-MS/MS. Over 100 Clp1-interacting proteins were consistently identified, over 70 of these were enriched in Clp1-C286S-TAP (potential substrates) and we and others detected Cdk1 phosphorylation sites in over half (44/73) of these potential substrates. According to GO annotations, Clp1-interacting proteins are involved in many essential cellular processes including mitosis, cytokinesis, ribosome biogenesis, transcription, and trafficking among others. We confirmed association and dephosphorylation of multiple candidate substrates, including a key scaffolding component of the septation initiation network called Cdc11, an essential kinase of the conserved morphogenesis-related NDR kinase network named Shk1, and multiple Mlu1-binding factor transcriptional regulators. In addition, we identified Sal3, a nuclear β-importin, as the sole karyopherin required for Clp1 nucleoplasmic shuttling, a key mode of Cdc14 phosphatase regulation. Finally, a handful of proteins were more abundant in wild type Clp1-TAP versus Clp1-C286S-TAP, suggesting that they may directly regulate Clp1 signaling or serve as scaffolding platforms to localize Clp1 activity.

Indexed as

Active Transport, Cell NucleusCDC2 Protein KinaseCell Cycle ProteinsCell NucleusKaryopherinsPeptide MappingPhosphorylationProtein Interaction MappingProtein Interaction MapsProtein Processing, Post-TranslationalProtein Tyrosine PhosphatasesProteomicsSchizosaccharomycesSchizosaccharomyces pombe ProteinsCDC11 protein, S pombeCDC2 Protein KinaseCell Cycle ProteinsClp1 protein, S. pombeKaryopherinsProtein Tyrosine PhosphatasesSchizosaccharomyces pombe Proteins

Identifiers

PMID23297348
PMCPMC3650322
OpenAlexW2171767753

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.