Evidence map›Paper›PMID 11782450›Full record

ArticleGenes & development2002

An ERK2 docking site in the Pointed domain distinguishes a subset of ETS transcription factors.

Jeffrey J Seidel, Barbara J Graves

Open access · diamondAbstract read
In one paragraph

Article in Genes & development, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.

0numbers the graph read from it
0cells of the map it votes in
80citing 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

80 citing papers in PubMed, 188 citations in OpenAlex.

  1. Article
  2. Article
  3. ETS1 Function in Leukemia and Lymphoma.Advances in experimental medicine and biology · 2024
    Review
  4. Article
  5. Article
  6. Sticky, Adaptable, and Many-sided: SAM protein versatility in normal and pathological hematopoietic states.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023
    Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Article

20 more citing papers are in PubMed but not listed here.

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

2 authors at 1 institution in 1 country.

Jeffrey J SeidelHuntsman Cancer Institute, Department of Oncological Sciences, University of Utah, Salt Lake City, Utah 84112-5550, USA.
Barbara J Graves
Huntsman Cancer Institute · US

Funding

UTAH REGIONAL CANCER CENTERP30CA042014 · NCI · UTAH STATE HIGHER EDUCATION SYSTEM--UNIVERSITY OF UTAH · PI CORNELIA M ULRICH · 1986 to 2026
$72.6M
Transcriptional Control Mechanisms by ETS FactorsR01GM038663 · NIGMS · UNIVERSITY OF UTAH · PI GRAVES, BARBARA J · 1992 to 2015
$3.9M
MULTIDISCPLINARY BASIC CANCER RESEARCH TRAININGT32CA009602 · NCI · UNIVERSITY OF UTAH · PI LEMONS, RICHARD S · 1988 to 1998
–
NCI NIH HHS CA09602NCI NIH HHS CA24014NCI NIH HHS T32 CA009602NIGMS NIH HHS R01 GM038663PHS HHS M38663
6 · The paper itself

Abstract

The ETS transcription factors perform distinct biological functions despite conserving a highly similar DNA-binding domain. One distinguishing property of a subset of ETS proteins is a conserved region of 80 amino acids termed the Pointed (PNT) domain. Using enzyme kinetics we determined that the Ets-1 PNT domain contains an ERK2 docking site. The docking site enhances the efficiency of phosphorylation of a mitogen-activated protein kinase (MAPK) site N-terminal to the PNT domain. The site enhances ERK2 binding rather than catalysis. Three hydrophobic residues are involved in docking, and the previously determined NMR structure indicates that these residues are clustered on the surface of the Ets-1 PNT domain. The docking site function is conserved in the PNT domain of the highly related Ets-2 but not in the ets family member GABPalpha. Ablation of the docking site in Ets-1 and Ets-2 prevented Ras pathway-mediated enhancement of the transactivation function of these proteins. This study provides structural insight into the function of a MAPK docking site and describes a unique activity for the PNT domain among a subset of ets family members.

Indexed as

3T3 CellsAnimalsBinding SitesMiceMitogen-Activated Protein Kinase 1PhosphorylationProto-Oncogene Protein c-ets-1Proto-Oncogene ProteinsProto-Oncogene Proteins c-etsTranscription FactorsEts1 protein, mouseMitogen-Activated Protein Kinase 1Proto-Oncogene Protein c-ets-1Proto-Oncogene ProteinsProto-Oncogene Proteins c-etsTranscription Factors

Identifiers

PMID11782450
PMCPMC155314
OpenAlexW2041798139

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.