Evidence map›Paper›PMID 8978819›Full record

ArticleThe Journal of cell biology1996

Exclusion of CD45 inhibits activity of p56lck associated with glycolipid-enriched membrane domains.

W Rodgers, J K Rose

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed
6.6field-weighted citation impact, top 3% 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

70 citing papers in PubMed, 307 citations in OpenAlex.

  1. Article
  2. Review
  3. Pre-organized landscape of T cell surface.Frontiers in immunology · 2023
    Review
  4. Review
  5. O-glycans direct selectin ligands to lipid rafts on leukocytes.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Functional role of gangliotetraosylceramide in epithelial-to-mesenchymal transition process induced by hypoxia and by TGF-{beta}.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2010
    Article
  14. Article
  15. Article
  16. T cell signal regulation by the actin cytoskeleton.The Journal of biological chemistry · 2010
    Article
  17. Article
  18. Cytoskeleton-membrane interactions in membrane raft structure.Cellular and molecular life sciences : CMLS · 2009
    Review
  19. Article
  20. Review

10 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.

W RodgersDepartment of Pathology, Yale University School of Medicine, New Haven, Connecticut 06510, USA.
J K Rose
Yale University · US

Funding

ASSEMBLY AND APPLICATION OF RECOMBINANT RHABDOVIRUSESR01AI024345 · NIAID · YALE UNIVERSITY · PI ROSE, JOHN · 1997 to 2001
$851k
RIBSOME RECOGNITION AND ANIMAL VIRUS GENE EXPRESSIONR37AI024345 · NIAID · YALE UNIVERSITY · PI ROSE, JOHN · 1987 to 1996
–
NIAID NIH HHS AI 24345
6 · The paper itself

Abstract

p56lck (Lck) is a lymphoid-specific Src family tyrosine kinase that is critical for T-cell development and activation. Lck is also a membrane protein, and approximately half of the membrane-associated Lck is associated with a glycolipid-enriched membrane (GEM) fraction that is resistant to solubilization by Triton X-100 (TX-100). To compare the membrane-associated Lck present in the GEM and TX-100-soluble fractions of Jurkat cells, Lck from each fraction was immunoblotted with antibody to phosphotyrosine. Lck in the GEM fraction was found to be hyperphosphorylated on tyrosine, and this correlated with a lower kinase specific activity relative to the TX-100-soluble Lck. Peptide mapping and phosphatase diagests showed that the hyperphosphorylation and lower kinase activity of GEM-associated Lck was due to phosphorylation of the regulatory COOH-terminal Tyr505. In addition, we determined that the membrane-bound tyrosine phosphatase CD45 was absent from the GEM fraction. Cells lacking CD45 showed identical phosphorylation of Lck in GEM and TX-100-soluble membranes. We propose that the GEM fraction represents a specific membrane domain present in T-cells, and that the hyperphosphorylation of tyrosine and lower kinase activity of GEM-associated Lck is due to exclusion of CD45 from these domains. Lck associated with the GEM domains may therefore consitute a reservoir of enzyme that can be readily activated.

Indexed as

Cell FractionationCell MembraneGlycolipidsHeLa CellsHumansJurkat CellsLeukocyte Common AntigensLymphocyte Specific Protein Tyrosine Kinase p56(lck)Membrane LipidsPhosphorylationsrc-Family KinasesTyrosineGlycolipidsLeukocyte Common AntigensLymphocyte Specific Protein Tyrosine Kinase p56(lck)Membrane Lipidssrc-Family KinasesTyrosine

Identifiers

PMID8978819
PMCPMC2133949
OpenAlexW2099593237

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.