Evidence map›Paper›PMID 24510915›Full record

ArticleThe EMBO journal2014

Co-regulation proteomics reveals substrates and mechanisms of APC/C-dependent degradation.

Sasha A Singh, Dominic Winter, Marc Kirchner, Ruchi Chauhan, Saima Ahmed, Nurhan Ozlu, Amit Tzur, Judith A Steen, Hanno Steen

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

49 citing papers in PubMed, 86 citations in OpenAlex.

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  20. SCFThe EMBO journal · 2021
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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

9 authors at 3 institutions in 3 countries.

Sasha A SinghDepartment of Pathology, Boston Children's Hospital and Harvard Medical School, Boston, MA, USA.
Dominic Winter
Marc Kirchner
Ruchi Chauhan
Saima Ahmed
Nurhan Ozlu
Amit Tzur
Judith A Steen
Hanno Steen
Boston Children's Hospital · USBar-Ilan University · ILKoç University · TR

Funding

SYNAPTIC MECHANISMS IN HIPPOCAMPAL EPILEPTOGENESISP30HD018655 · NICHD · CHILDREN'S HOSPITAL BOSTON · PI POMEROY, SCOTT LOREN · 1985 to 2015
$26.2M
CORE--ZEBRAFISHP30DK049216 · NIDDK · CHILDREN'S HOSPITAL BOSTON · PI ORKIN, STUART H · 1999 to 2015
$14.3M
Regulation of SMN and Identification of its Downstream TargetR01NS066973 · NINDS · BOSTON CHILDREN'S HOSPITAL · PI STEEN, JUDITH A · 2010 to 2014
$2.2M
Defining the true nature of the minimal cell cycle with quantitative proteomicsR01GM094844 · NIGMS · BOSTON CHILDREN'S HOSPITAL · PI STEEN, HANNO · 2010 to 2013
$1.4M
NICHD NIH HHS P30 HD018655NICHD NIH HHS P30 HD18655NIDDK NIH HHS P30 DK049216NIGMS NIH HHS R01 GM094844NINDS NIH HHS R01 NS066973
6 · The paper itself

Abstract

Using multiplexed quantitative proteomics, we analyzed cell cycle-dependent changes of the human proteome. We identified >4,400 proteins, each with a six-point abundance profile across the cell cycle. Hypothesizing that proteins with similar abundance profiles are co-regulated, we clustered the proteins with abundance profiles most similar to known Anaphase-Promoting Complex/Cyclosome (APC/C) substrates to identify additional putative APC/C substrates. This protein profile similarity screening (PPSS) analysis resulted in a shortlist enriched in kinases and kinesins. Biochemical studies on the kinesins confirmed KIFC1, KIF18A, KIF2C, and KIF4A as APC/C substrates. Furthermore, we showed that the APC/C(CDH1)-dependent degradation of KIFC1 regulates the bipolar spindle formation and proper cell division. A targeted quantitative proteomics experiment showed that KIFC1 degradation is modulated by a stabilizing CDK1-dependent phosphorylation site within the degradation motif of KIFC1. The regulation of KIFC1 (de-)phosphorylation and degradation provides insights into the fidelity and proper ordering of substrate degradation by the APC/C during mitosis.

Indexed as

ProteolysisProteomicsAmino Acid SequenceAnaphase-Promoting Complex-CyclosomeCell CycleHeLa CellsHumansKinesinsModels, BiologicalMolecular Sequence DataPhosphorylationRecombinant Fusion ProteinsSubstrate SpecificityUbiquitinationAnaphase-Promoting Complex-CyclosomeKIF18A protein, humanKIFC1 protein, humanKinesinsRecombinant Fusion Proteins

Identifiers

PMID24510915
PMCPMC3989644
OpenAlexW2147068611

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.