Evidence map›Paper›PMID 11689425›Full record

ArticleThe EMBO journal2001

Structural basis for the interaction of the free SH2 domain EAT-2 with SLAM receptors in hematopoietic cells.

M Morra, J Lu, F Poy, M Martin, J Sayos, S Calpe, C Gullo, D Howie, S Rietdijk, A Thompson and 6 more

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
2.5field-weighted citation impact, top 10% 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

50 citing papers in PubMed, 147 citations in OpenAlex.

  1. Review
  2. Powerful mapping ofmedRxiv : the preprint server for health sciences · 2024
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  3. Review
  4. SLAM Family Receptors in B Cell Chronic Lymphoproliferative Disorders.International journal of molecular sciences · 2024
    Review
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  14. Observational
  15. Article
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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

16 authors at 1 institution in 1 country.

M MorraDivision of Immunology, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA 02115, USA. mmorra@caregroup.harvard.edu
J Lu
F Poy
M Martin
J Sayos
S Calpe
C Gullo
D Howie
S Rietdijk
A Thompson
A J Coyle
C Denny
M B Yaffe
P Engel
M J Eck
C Terhorst
Harvard University · US

Funding

TRANSGENIC MODELS OF T CELL RECEPTOR IMMUNODEFICIENCIESP01AI035714 · NIAID · BETH ISRAEL DEACONESS MEDICAL CENTER · PI TERHORST, CORNELIS P · 1994 to 2007
$9.3M
NIAID NIH HHS P01 AI035714NIAID NIH HHS P01-AI-35714
6 · The paper itself

Abstract

The T and natural killer (NK) cell-specific gene SAP (SH2D1A) encodes a 'free SH2 domain' that binds a specific tyrosine motif in the cytoplasmic tail of SLAM (CD150) and related cell surface proteins. Mutations in SH2D1A cause the X-linked lymphoproliferative disease, a primary immunodeficiency. Here we report that a second gene encoding a free SH2 domain, EAT-2, is expressed in macrophages and B lympho cytes. The EAT-2 structure in complex with a phosphotyrosine peptide containing a sequence motif with Tyr281 of the cytoplasmic tail of CD150 is very similar to the structure of SH2D1A complexed with the same peptide. This explains the high affinity of EAT-2 for the pTyr motif in the cytoplasmic tail of CD150 but, unlike SH2D1A, EAT-2 does not bind to non-phosphorylated CD150. EAT-2 binds to the phosphorylated receptors CD84, CD150, CD229 and CD244, and acts as a natural inhibitor, which interferes with the recruitment of the tyrosine phosphatase SHP-2. We conclude that EAT-2 plays a role in controlling signal transduction through at least four receptors expressed on the surface of professional antigen-presenting cells.

Indexed as

Blood Coagulation FactorsIntracellular Signaling Peptides and ProteinsModels, MolecularAdaptor Proteins, Signal TransducingAmino Acid MotifsAnimalsAntigens, CDBase SequenceB-LymphocytesCarrier ProteinsCOS CellsGlycoproteinsHumansImmunoglobulinsMacromolecular SubstancesMacrophagesactivated protein C receptorAdaptor Proteins, Signal TransducingAntigens, CDBlood Coagulation FactorsCarrier ProteinsFYN protein, humanFyn protein, mouseGlycoproteinsImmunoglobulinsIntracellular Signaling Peptides and ProteinsMacromolecular SubstancesProtein Tyrosine Phosphatase, Non-Receptor Type 11Protein Tyrosine Phosphatase, Non-Receptor Type 6Protein Tyrosine PhosphatasesProto-Oncogene ProteinsProto-Oncogene Proteins c-fynPTPN11 protein, humanPtpn11 protein, mousePTPN6 protein, humanPtpn6 protein, mouseReceptors, Cell SurfaceSH2D1A protein, humanSh2d1a protein, mouseSh2d1b1 protein, mouseSH2D1B protein, humanSH2 Domain-Containing Protein Tyrosine PhosphatasesSignaling Lymphocytic Activation Molecule Associated ProteinSignaling Lymphocytic Activation Molecule Family Member 1SLAMF1 protein, humanTranscription Factors

Identifiers

PMID11689425
PMCPMC125701
OpenAlexW2117690348

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.