Evidence map›Paper›PMID 24842995›Full record

ArticleeLife2014

RNAP II CTD tyrosine 1 performs diverse functions in vertebrate cells.

Jing-Ping Hsin, Wencheng Li, Mainul Hoque, Bin Tian, James L Manley

Open access · goldAbstract read
In one paragraph

Article in eLife, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

35 citing papers in PubMed, 51 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Review
  10. Article
  11. Review
  12. Ssu72 Dual-Specific Protein Phosphatase: From Gene to Diseases.International journal of molecular sciences · 2021
    Review
  13. Review
  14. Enhancer RNAs are an important regulatory layer of the epigenome.Nature structural & molecular biology · 2020
    Review
  15. Review
  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

5 authors at 3 institutions in 1 country.

Jing-Ping HsinDepartment of Biological Sciences, Columbia University, New York, United States.
Wencheng LiDepartment of Biochemistry and Molecular Biology, Rutgers University New Jersey Medical School, Newark, United States.
Mainul HoqueDepartment of Biochemistry and Molecular Biology, Rutgers University New Jersey Medical School, Newark, United States.
Bin TianDepartment of Biochemistry and Molecular Biology, Rutgers University New Jersey Medical School, Newark, United States.
James L ManleyDepartment of Biological Sciences, Columbia University, New York, United States jlm2@columbia.edu.
Columbia University · USRutgers New Jersey Medical SchoolRutgers, The State University of New Jersey · US

Funding

Regulation of Alternative Cleavage and PolyadenylationR01GM084089 · NIGMS · WISTAR INSTITUTE · PI TIAN, BIN · 2008 to 2023
$6.7M
Transcriptional regulation by protein sumoylationR01GM097174 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI MANLEY, JAMES L. · 2011 to 2014
$990k
NIGMS NIH HHS GM084089NIGMS NIH HHS GM097174NIGMS NIH HHS R01 GM084089NIGMS NIH HHS R01 GM097174
6 · The paper itself

Abstract

The RNA polymerase II largest subunit (Rpb1) contains a unique C-terminal domain (CTD) that plays multiple roles during transcription. The CTD is composed of consensus Y(1)S(2)P(3)T(4)S(5)P(6)S(7) repeats, in which Ser, Thr and Tyr residues can all be phosphorylated. Here we report analysis of CTD Tyr1 using genetically tractable chicken DT40 cells. Cells expressing an Rpb1 derivative with all Tyr residues mutated to Phe (Rpb1-Y1F) were inviable. Remarkably, Rpb1-Y1F was unstable, degraded to a CTD-less form; however stability, but not cell viability, was fully rescued by restoration of a single C-terminal Tyr (Rpb1-25F+Y). Cytoplasmic and nucleoplasmic Rpb1 was phosphorylated exclusively on Tyr1, and phosphorylation specifically of Tyr1 prevented CTD degradation by the proteasome in vitro. Tyr1 phosphorylation was also detected on chromatin-associated, hyperphosphorylated Rpb1, consistent with a role in transcription. Indeed, we detected accumulation of upstream antisense (ua) RNAs in Rpb1-25F+Y cells, indicating a role for Tyr1 in uaRNA expression.DOI: http://dx.doi.org/10.7554/eLife.02112.001.

Indexed as

AnimalsCell LineChickensPhosphorylationRNA Polymerase IITyrosineRNA Polymerase IITyrosineCTDproteasomeRNA polymerase IIRpb1 protein stabilitytyrosineupstream antisense RNA

Identifiers

PMID24842995
PMCPMC4042873
OpenAlexW2149010133

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.