Evidence map›Paper›PMID 9857189›Full record

ArticleThe EMBO journal1998

A cdc15-like adaptor protein (CD2BP1) interacts with the CD2 cytoplasmic domain and regulates CD2-triggered adhesion.

J Li, K Nishizawa, W An, R E Hussey, F E Lialios, R Salgia, R Sunder-Plassmann, E L Reinherz

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.2field-weighted citation impact, top 11% 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

22 citing papers in PubMed, 101 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. CD2 Immunobiology.Frontiers in immunology · 2020
    Review
  6. Deciphering the BAR code of membrane modulators.Cellular and molecular life sciences : CMLS · 2017
    Review
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Pyrin binds the PSTPIP1/CD2BP1 protein, defining familial Mediterranean fever and PAPA syndrome as disorders in the same pathway.Proceedings of the National Academy of Sciences of the United States of America · 2003
    Article
  16. NOSTRIN: a protein modulating nitric oxide release and subcellular distribution of endothelial nitric oxide synthase.Proceedings of the National Academy of Sciences of the United States of America · 2002
    Article
  17. Article
  18. CD2 molecules redistribute to the uropod during T cell scanning: implications for cellular activation and immune surveillance.Proceedings of the National Academy of Sciences of the United States of America · 2002
    Article
  19. Article
  20. A subtle role for CD2 in T cell antigen recognition.The Journal of experimental medicine · 1999
    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

8 authors at 1 institution in 1 country.

J LiLaboratory of Immunobiology, Harvard Medical School, 44 Binney Street J318, Boston, MA 02115, USA.
K Nishizawa
W An
R E Hussey
F E Lialios
R Salgia
R Sunder-Plassmann
E L Reinherz
Harvard University · US

Funding

GENES ENCODING THE T CELL ANTIGEN RECEPTORR01AI021226 · NIAID · DANA-FARBER CANCER INSTITUTE · PI REINHERZ, ELLIS L · 1985 to 2006
$3.8M
NIAID NIH HHS AI21226
6 · The paper itself

Abstract

A human CD2 cytoplasmic tail-binding protein, termed CD2BP1, was identified by an interaction trap cloning method. Expression of CD2BP1 is restricted to hematopoietic tissue, being prominent in T and natural killer (NK) cells, with long (CD2BP1L) and short (CD2BP1S) variants arising by alternative RNA splicing. Both CD2BP1 molecules are homologous to Schizosaccharomyces pombe cdc15, and include a helical domain, variable length intervening PEST sequence and C-terminal SH3 domain. Although the CD2BP1 SH3 domain binds directly to the CD2 sequence, KGPPLPRPRV (amino acids 300-309), its association is augmented markedly by the CD2BP1 N-terminal segment. Upon ligand-induced clustering of surface CD2 molecules, CD2BP1 redistributes from a cytosolic to a surface membrane compartment, co-localizing with CD2. In turn, CD2-stimulated adhesion is downregulated by CD2BP1, apparently through coupling of the protein tyrosine phosphatase (PTP)-PEST to CD2. These findings offer the first molecular view into the control processes for T cell adhesion.

Indexed as

Cell AdhesionAlternative SplicingAmino Acid SequenceBinding SitesCD2 AntigensCD58 AntigensCell Cycle ProteinsCell PolarityCloning, MolecularCytoplasmGTP-Binding ProteinsHumansImmunologic CappingLeukocytesMolecular Sequence DataProtein BindingCD2 AntigensCD58 AntigensCDC15 proteinCell Cycle ProteinsGTP-Binding ProteinsProtein Tyrosine Phosphatase, Non-Receptor Type 12Protein Tyrosine PhosphatasesPTPN12 protein, human

Identifiers

PMID9857189
PMCPMC1171078
OpenAlexW2116517185

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.