Evidence map›Paper›PMID 18829461›Full record

ArticleThe Journal of biological chemistry2008

Phosphatase PPM1A regulates phosphorylation of Thr-186 in the Cdk9 T-loop.

Yan Wang, Eugene C Dow, Yao-Yun Liang, Rajesh Ramakrishnan, Hongbing Liu, Tzu-Ling Sung, Xia Lin, Andrew P Rice

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

46 citing papers in PubMed, 74 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. A comprehensive overview of PPM1A: From structure to disease.Experimental biology and medicine (Maywood, N.J.) · 2022
    Review
  5. CDK9 keeps RNA polymerase II on track.Cellular and molecular life sciences : CMLS · 2021
    Review
  6. Knockdown of MgExperimental and therapeutic medicine · 2020
    Article
  7. P-TEFb as A Promising Therapeutic Target.Molecules (Basel, Switzerland) · 2020
    Review
  8. Review
  9. Review
  10. Article
  11. Review
  12. Article
  13. Review
  14. Review
  15. Cyclin Dependent Kinase 9 Inhibitors for Cancer Therapy.Journal of medicinal chemistry · 2016
    Article
  16. Review
  17. P-TEFb goes viral.Inside the cell · 2016
    Review
  18. Article
  19. Article
  20. Review
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 at 1 institution in 1 country.

Yan WangDepartment of Molecular Virology and Microbiology, Baylor College of Medicine, Houston, Texas 77030, USA.
Eugene C Dow
Yao-Yun Liang
Rajesh Ramakrishnan
Hongbing Liu
Tzu-Ling Sung
Xia Lin
Andrew P Rice
Baylor College of Medicine · US

Funding

Mechanisms of HIV-1 latency in CD4+ T lymphocytesR01AI035381 · NIAID · BAYLOR COLLEGE OF MEDICINE · PI RICE, ANDREW P · 1995 to 2007
$2.5M
Regulation of SMAD2 Signaling by SMP1 PhosphataseR01DK073932 · NIDDK · BAYLOR COLLEGE OF MEDICINE · PI LIN, XIA · 2005 to 2008
$1.1M
Mechanism of HIV-1 Tat FunctionR56AI035381 · NIAID · BAYLOR COLLEGE OF MEDICINE · PI RICE, ANDREW P · 2009 to 2009
$384k
NIAID NIH HHS AI35381NIDDK NIH HHS DK073932
6 · The paper itself

Abstract

Cdk9 is the catalytic subunit of a general RNA polymerase II elongation factor known as positive transcription elongation factor b (P-TEFb). The kinase function of P-TEFb requires phosphorylation of Thr-186 in the T-loop of Cdk9 to allow substrates to access the catalytic core of the enzyme. To identify human phosphatases that dephosphorylate the T-loop of Cdk9, we used a Thr-186-phosphospecific antiserum to screen a phosphatase expression library. Overexpression of PPM1A and the related PPM1B greatly reduced Cdk9 T-loop phosphorylation in vivo. PPM1A and Cdk9 appear to associate in vivo as the proteins could be co-immunoprecipitated. The short hairpin RNA depletion of PPM1A resulted in an increase in Cdk9 T-loop phosphorylation. In phosphatase reactions in vitro, purified PPM1A could dephosphorylate Thr-186 both with and without the association of 7SK RNA, a small nuclear RNA that is bound to approximately 50% of total cellular P-TEFb. PPM1B only efficiently dephosphorylated Cdk9 Thr-186 in vitro when 7SK RNA was depleted from P-TEFb. Taken together, our data indicate that PPM1A and to some extent PPM1B are important negative regulators of P-TEFb function.

Indexed as

Catalytic DomainCyclin-Dependent Kinase 9HeLa CellsHumansPhosphoprotein PhosphatasesPhosphorylationPositive Transcriptional Elongation Factor BProtein Phosphatase 2CProtein Structure, SecondaryRNA, Small NuclearCDK9 protein, humanCyclin-Dependent Kinase 9Phosphoprotein PhosphatasesPositive Transcriptional Elongation Factor BPPM1A protein, humanPPM1B protein, humanProtein Phosphatase 2CRNA, Small Nuclear

Identifiers

PMID18829461
PMCPMC2586277
OpenAlexW2024317868

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.