Evidence map›Paper›PMID 18583928›Full record

ArticleCell cycle (Georgetown, Tex.)2008

Cell cycle-dependent phosphorylation of human CDC5 regulates RNA processing.

Remo Gräub, Hope Lancero, Anissa Pedersen, Meihua Chu, Krishnan Padmanabhan, Xiao-Qin Xu, Paul Spitz, Robert Chalkley, Alma L Burlingame, David Stokoe and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Cell cycle (Georgetown, Tex.), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

14 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Review
  3. DNA and RNA Binding Proteins: From Motifs to Roles in Cancer.International journal of molecular sciences · 2022
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Molecular architecture of the human Prp19/CDC5L complex.Molecular and cellular biology · 2010
    Article
  14. Article
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

11 authors at 1 institution in 1 country.

Remo GräubCardiovascular Research Institute, University of California, San Francisco, CA 94143-0130, USA.
Hope Lancero
Anissa Pedersen
Meihua Chu
Krishnan Padmanabhan
Xiao-Qin Xu
Paul Spitz
Robert Chalkley
Alma L Burlingame
David Stokoe
Harold S Bernstein
University of California, San Francisco · US

Funding

YEAST THREONINE &SERINE KINASESP41RR001614 · NCRR · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI ORTIZ DE MONTELLANO, PAUL R · 1985 to 2011
$24.1M
Training in Developmental Cardiovascular BiologyT32HL007544 · NHLBI · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI SRIVASTAVA, DEEPAK · 1985 to 2021
$4.5M
CELL CYCLE REGULATION IN CARDIOVASCULAR BIOLOGYR01HL062174 · NHLBI · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI BERNSTEIN, HAROLD S · 1999 to 2003
$1.1M
NCRR NIH HHS P41 RR001614NCRR NIH HHS RR01614NHLBI NIH HHS HL007544NHLBI NIH HHS HL062174NHLBI NIH HHS R01 HL062174NHLBI NIH HHS T32 HL007544
6 · The paper itself

Abstract

CDC5 proteins are components of the pre-mRNA splicing complex and essential for cell cycle progression in yeast, plants and mammals. Human CDC5 is phosphorylated in a mitogen-dependent manner, and its association with the spliceosome is ATP-dependent. Examination of the amino acid sequence suggests that CDC5L may be phosphorylated at up to 28 potential consensus recognition sequences for known kinases, however, the identity of actual phosphorylation sites, their role in regulating CDC5L activity, and the kinases responsible for their phosphorylation have not previously been determined. Using two-dimensional phosphopeptide mapping and nanoelectrospray mass spectrometry, we now show that CDC5L is phosphorylated on at least nine sites in vivo. We demonstrate that while CDC5L is capable of forming homodimers in vitro and in vivo, neither homodimerization nor nuclear localization is dependent on phosphorylation at these sites. Using an in vitro splicing assay, we show that phosphorylation of CDC5L at threonines 411 and 438 within recognition sequences for CDKs are required for CDC5L-mediated pre-mRNA splicing. We also demonstrate that a specific inhibitor of CDK2, CVT-313, inhibits CDC5L phosphorylation in both in vitro kinase assays and in vivo radiolabeling experiments in cycling cells. These studies represent the first demonstration of a regulatory role for phosphorylation of CDC5L, and suggest that targeting these sites or the implicated kinases may provide novel strategies for treating disorders of unguarded cellular proliferation, such as cancer.

Indexed as

Cell CycleRNA Processing, Post-TranscriptionalAnimalsCell Cycle ProteinsCell NucleusChlorocebus aethiopsCOS CellsDimerizationEnzyme InhibitorsHumansPeptide MappingPhosphorylationPurinesRNA-Binding ProteinsCDC5L protein, humanCell Cycle ProteinsCVT 313Enzyme InhibitorsPurinesRNA-Binding Proteins

Identifiers

PMID18583928
PMCPMC2940709
OpenAlexW2019600767

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.