Evidence map›Paper›PMID 17488287›Full record

ArticleTraffic (Copenhagen, Denmark)2007

A GAPDH mutant defective in Src-dependent tyrosine phosphorylation impedes Rab2-mediated events.

Ellen J Tisdale, Cristina R Artalejo

Abstract read
In one paragraph

Article in Traffic (Copenhagen, Denmark), 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

24 citing papers in PubMed, 57 citations in OpenAlex.

  1. Trial
  2. Article
  3. Review
  4. Review
  5. Article
  6. MAP1203 PromotesFrontiers in cellular and infection microbiology · 2018
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. GAPDH regulates cellular heme insertion into inducible nitric oxide synthase.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  18. Article
  19. Article
  20. 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

2 authors at 1 institution in 1 country.

Ellen J TisdaleDepartment of Pharmacology, Wayne State University School of Medicine, 540 East Canfield Avenue, 6374 Scott Hall, Detroit, MI 48201, USA. etisdale@med.wayne.edu
Cristina R Artalejo
Wayne State University · US

Funding

VTC Events Mediated by the Rab2 ComplexR01GM068813 · NIGMS · WAYNE STATE UNIVERSITY · PI TISDALE, ELLEN J · 2005 to 2010
$1.2M
DISSECTION OF CAPS FUNCTION IN CHROMAFFIN CELL SECRETIONR01DK057637 · NIDDK · WAYNE STATE UNIVERSITY · PI ARTALEJO, CRISTINA R · 2001 to 2004
$900k
REGULATION OF ENDOCYTOSIS IN NEUROENDOCRINE CELLSR01DK058921 · NIDDK · WAYNE STATE UNIVERSITY · PI ARTALEJO, CRISTINA R · 2001 to 2004
$880k
NIDDK NIH HHS DK57637NIDDK NIH HHS DK58921NIDDK NIH HHS R01 DK057637NIDDK NIH HHS R01 DK058921NIGMS NIH HHS R01 GM068813
6 · The paper itself

Abstract

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) has multiple intracellular activities in addition to its role in gluconeogenesis. Indeed, we have reported that GAPDH is required for Rab2-mediated retrograde transport from vesicular tubular clusters (VTCs). These diverse GAPDH activities are the result of posttranslational modifications that confer a new function to the enzyme. In that regard, GAPDH is tyrosine phosphorylated by Src. To establish the functional significance of this modification for GAPDH activity in Rab2-dependent events, an amino acid substitution was made at tyrosine 41 (GAPDH Y41F). The inability of Src to phosphorylate purified recombinant GAPDH Y41F was confirmed in an in vitro kinase assay. The mutant was then employed in a quantitative membrane-binding assay that measures Rab2 recruitment of soluble components to VTCs. As we observed with GAPDH wild type, Rab2 promoted GAPDH Y41F binding to membranes in a dose-dependent manner, indicating that GAPDH tyrosine phosphorylation is not required for VTC association. However, GAPDH was tyrosine phosphorylated on VTCs. Importantly, GAPDH Y41F blocked vesicular stomatitis virus-G transport in an assay that reconstitutes endoplasmic reticulum to Golgi trafficking, indicating that phosphorylation of tyrosine 41 is essential for GAPDH activity in the early secretory pathway. The block in transport is because of the decreased binding of atypical protein kinase C iota/lambda to GAPDH Y41F, which reduces beta-coat protein association with the VTC and subsequent formation of Rab2-mediated retrograde vesicles. Our results suggest that Src plays a pivotal role in regulating the interaction of Rab2 effectors on the VTC.

Indexed as

Amino Acid SubstitutionAnimalsCell LineCytoplasmic VesiclesFluorescent Antibody Technique, IndirectGlyceraldehyde-3-Phosphate DehydrogenasesModels, BiologicalPhosphorylationProtein Transportrab2 GTP-Binding ProteinRatsRecombinant Proteinssrc-Family KinasesTyrosineGlyceraldehyde-3-Phosphate Dehydrogenasesrab2 GTP-Binding ProteinRecombinant Proteinssrc-Family KinasesTyrosine

Identifiers

PMID17488287
PMCPMC3775588
OpenAlexW2084146928

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.