Evidence map›Paper›PMID 24752900›Full record

ArticleMolecular and cellular biology2014

Function and control of RNA polymerase II C-terminal domain phosphorylation in vertebrate transcription and RNA processing.

Jing-Ping Hsin, Kehui Xiang, James L Manley

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
3.8field-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

40 citing papers in PubMed, 53 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Review
  14. Review
  15. JMJD5 couples with CDK9 to release the paused RNA polymerase II.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  16. Article
  17. Article
  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

3 authors at 1 institution in 1 country.

Jing-Ping HsinDepartment of Biological Sciences, Columbia University, New York, New York, USA.
Kehui XiangDepartment of Biological Sciences, Columbia University, New York, New York, USA.
James L ManleyDepartment of Biological Sciences, Columbia University, New York, New York, USA jlm2@columbia.edu.
Columbia University · US

Funding

Transcriptional regulation by protein sumoylationR01GM097174 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI MANLEY, JAMES L. · 2011 to 2014
$990k
NIGMS NIH HHS R01 GM097174NIGMS NIH HHS R01GM097174
6 · The paper itself

Abstract

The C-terminal domain of the RNA polymerase II largest subunit (the Rpb1 CTD) is composed of tandem heptad repeats of the consensus sequence Y(1)S(2)P(3)T(4)S(5)P(6)S(7). We reported previously that Thr 4 is phosphorylated and functions in histone mRNA 3'-end formation in chicken DT40 cells. Here, we have extended our studies on Thr 4 and to other CTD mutations by using these cells. We found that an Rpb1 derivative containing only the N-terminal half of the CTD, as well as a similar derivative containing all-consensus repeats (26r), conferred full viability, while the C-terminal half, with more-divergent repeats, did not, reflecting a strong and specific defect in snRNA 3'-end formation. Mutation in 26r of all Ser 2 (S2A) or Ser 5 (S5A) residues resulted in lethality, while Ser 7 (S7A) mutants were fully viable. While S2A and S5A cells displayed defects in transcription and RNA processing, S7A cells behaved identically to 26r cells in all respects. Finally, we found that Thr 4 was phosphorylated by cyclin-dependent kinase 9 in cells and dephosphorylated both in vitro and in vivo by the phosphatase Fcp1.

Indexed as

RNA Processing, Post-TranscriptionalAmino Acid SequenceAnimalsCell LineChickensCyclin-Dependent Kinase 9HEK293 CellsHumansMutationPhosphoprotein PhosphatasesPhosphorylationProtein SubunitsRNA Polymerase IIRNA, Small NuclearThreonineTranscription, GeneticCDK9 protein, humanCyclin-Dependent Kinase 9Fcp1 protein, humanPhosphoprotein PhosphatasesProtein SubunitsRNA Polymerase IIRNA polymerase II largest subunitRNA, Small NuclearThreonine

Identifiers

PMID24752900
PMCPMC4054314
OpenAlexW2134290451

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.