Evidence map›Paper›PMID 20506281›Full record

ArticleJournal of cellular biochemistry2010

Fyn promotes phosphorylation of collapsin response mediator protein 1 at tyrosine 504, a novel, isoform-specific regulatory site.

Gwen R Buel, John Rush, Bryan A Ballif

Abstract read
In one paragraph

Article in Journal of cellular biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
0.6field-weighted citation impact, top 38% 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

18 citing papers in PubMed, 23 citations in OpenAlex.

  1. Case report: AFrontiers in neuroscience · 2024
    Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Article
  18. 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 2 institutions in 1 country.

Gwen R BuelDepartment of Biology, University of Vermont, 120A Marsh Life Science Building, 109 Carrigan Drive, Burlington, Vermont 05405, USA.
John Rush
Bryan A Ballif
University of Vermont · USCell Signaling Technology (United States) · US

Funding

VOLATILE SIGNALING IN PHARBITIS NILP20RR016462 · NCRR · UNIVERSITY OF VERMONT &ST AGRIC COLLEGE · PI VAN HOUTEN, JUDITH L · 2001 to 2011
$31.1M
NCRR NIH HHS P20 RR016462NCRR NIH HHS P20 RR16462
6 · The paper itself

Abstract

In vertebrates the collapsin response mediator proteins (CRMPs) are encoded by five highly related genes. CRMPs are cytosolic phosphoproteins abundantly expressed in developing and mature mammalian brains. CRMPs are best understood as effectors of Semaphorin 3A signaling regulating growth cone collapse in migratory neurons. Phosphorylation in the carboxyl-terminal regulatory domain of CRMPs by several serine/threonine kinases has been described. These phoshorylation events appear to function, at least in part, to disrupt the interaction of CRMPs with tubulin heterodimers. In a large-scale phosphoproteomic analysis of murine brain, we recently identified a number of in vivo tyrosine phosphorylation sites on CRMP isoforms. Using biochemical approaches and quantitative mass spectrometry we demonstrate that one of these sites, CRMP1 tyrosine 504 (Y504), is a primary target of the Src family of tyrosine kinases (SFKs), specifically Fyn. Y504 is adjacent to CDK5 and GSK-3beta sites that regulate the interaction of CRMPs with tubulin. Although Y504 is highly conserved among vertebrate CRMP1 orthologs, a residue corresponding to Y504 is absent in CRMP isoforms 2-5. This suggests an isoform-specific regulatory role for CRMP1 Y504 phosphorylation and may help explain the observation that CRMP1-deficient mice exhibit neuronal migration defects not compensated for by CRMPs 2-5.

Indexed as

Amino Acid SequenceAnimalsCollapsin Response Mediator Protein 1HEK293 CellsHumansHydrogen PeroxideMiceMolecular Sequence DataNerve Tissue ProteinsOxidantsPhosphoproteinsPhosphorylationProtein IsoformsProto-Oncogene Proteins c-fynSequence AlignmentTyrosineCollapsin Response Mediator Protein 1Fyn protein, mouseHydrogen PeroxideNerve Tissue ProteinsOxidantsPhosphoproteinsProtein IsoformsProto-Oncogene Proteins c-fynTyrosine

Identifiers

PMID20506281
PMCPMC4198339
OpenAlexW2100543943

What Socratic holds

Textmetadata
LicenceTDM
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 Socratic graph.