Evidence map›Paper›PMID 20663872›Full record

ArticleThe Journal of biological chemistry2010

B55alpha PP2A holoenzymes modulate the phosphorylation status of the retinoblastoma-related protein p107 and its activation.

Girish Jayadeva, Alison Kurimchak, Judit Garriga, Elena Sotillo, Anthony J Davis, Dale S Haines, Marc Mumby, Xavier Graña

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing 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

27 citing papers in PubMed.

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  14. Leucine-rich repeat-containing protein 59 mediates nuclear import of cancerous inhibitor of PP2A in prostate cancer cells.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2015
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  19. Upregulation of miR-136 in human non-small cell lung cancer cells promotes Erk1/2 activation by targeting PPP2R2A.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2014
    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

8 authors.

Girish JayadevaFels Institute for Cancer Research and Molecular Biology, Temple University School of Medicine, Philadelphia, Pennsylvania 19140, USA.
Alison Kurimchak
Judit Garriga
Elena Sotillo
Anthony J Davis
Dale S Haines
Marc Mumby
Xavier Graña

Funding

G1 Cell Cycle in Tumorigenesis and SenescenceP01CA095569 · NCI · TEMPLE UNIV OF THE COMMONWEALTH · PI REDDY, E PREMKUMAR · 2003 to 2007
$6.1M
Cell cycle regulation by protein phosphatase 2AR01GM086560 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI MUMBY, MARC C. · 2009 to 2012
$1.2M
T-TYPE CYCLIN/CDK9 COMPLEXES IN T CELL ACTIVATIONK02AI001823 · NIAID · TEMPLE UNIVERSITY · PI GRANA, XAVIER · 2000 to 2004
$522k
NCI NIH HHS CA095569NCI NIH HHS P01 CA095569NIAID NIH HHS K02 AI001823NIAID NIH HHS K02 AI01823NIGMS NIH HHS R01 GM086560
6 · The paper itself

Abstract

Pocket proteins negatively regulate transcription of E2F-dependent genes and progression through the G(0)/G(1) transition and the cell cycle restriction point in G(1). Pocket protein repressor activities are inactivated via phosphorylation at multiple Pro-directed Ser/Thr sites by the coordinated action of G(1) and G(1)/S cyclin-dependent kinases. These phosphorylations are reversed by the action of two families of Ser/Thr phosphatases: PP1, which has been implicated in abrupt dephosphorylation of retinoblastoma protein (pRB) in mitosis, and PP2A, which plays a role in an equilibrium that counteracts cyclin-dependent kinase (CDK) action throughout the cell cycle. However, the identity of the trimeric PP2A holoenzyme(s) functioning in this process is unknown. Here we report the identification of a PP2A trimeric holoenzyme containing B55α, which plays a major role in restricting the phosphorylation state of p107 and inducing its activation in human cells. Our data also suggest targeted selectivity in the interaction of pocket proteins with distinct PP2A holoenzymes, which is likely necessary for simultaneous pocket protein activation.

Indexed as

Cell CycleCell Line, TumorCyclin-Dependent KinasesE2F Transcription FactorsHoloenzymesHumansPhosphorylationProtein MultimerizationProtein Phosphatase 2Retinoblastoma-Like Protein p107Transcription, GeneticCyclin-Dependent KinasesE2F Transcription FactorsHoloenzymesPPP2CA protein, humanProtein Phosphatase 2RBL1 protein, humanRetinoblastoma-Like Protein p107

Identifiers

PMID20663872
PMCPMC2943288

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.