Evidence map›Paper›PMID 25587033›Full record

ArticleMolecular & cellular proteomics : MCP2015

Tyrosine phosphorylation of the Lyn Src homology 2 (SH2) domain modulates its binding affinity and specificity.

Lily L Jin, Leanne E Wybenga-Groot, Jiefei Tong, Paul Taylor, Mark D Minden, Suzanne Trudel, C Jane McGlade, Michael F Moran

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing 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

25 citing papers in PubMed, 41 citations in OpenAlex.

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  13. SH2 Domain Binding: Diverse FLVRs of Partnership.Frontiers in endocrinology · 2020
    Review
  14. Article
  15. Article
  16. Article
  17. TCR Signaling: Mechanisms of Initiation and Propagation.Trends in biochemical sciences · 2018
    Review
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  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

8 authors at 6 institutions in 2 countries.

Lily L JinFrom the ‡Molecular Structure and Function, The Hospital For Sick Children, 686 Bay Street, Toronto, M5G 0A4, Canada; ‡‡Departments of Molecular Genetics, Medical Science Building, Room 4386, 1 King's College Circle, Toronto, ON M5S 1A8, Canada;
Leanne E Wybenga-Groot§Cell Biology, The Hospital For Sick Children, 686 Bay Street, Toronto, M5G 0A4, Canada; ¶The Arthur and Sonia Labatt Brain Tumour Research Centre, The Hospital For Sick Children, 686 Bay Street, Toronto, M5G 0A4, Canada;
Jiefei TongFrom the ‡Molecular Structure and Function, The Hospital For Sick Children, 686 Bay Street, Toronto, M5G 0A4, Canada;
Paul TaylorFrom the ‡Molecular Structure and Function, The Hospital For Sick Children, 686 Bay Street, Toronto, M5G 0A4, Canada;
Mark D Minden‖Medical Biophysics, University of Toronto, Medical Science Building, Room 4386, 1 King's College Circle, Toronto, ON M5S 1A8, Canada; **The Princess Margaret Cancer Center, 610 University Avenue, M5G 2M9, Toronto, Canada.
Suzanne Trudel‖Medical Biophysics, University of Toronto, Medical Science Building, Room 4386, 1 King's College Circle, Toronto, ON M5S 1A8, Canada; **The Princess Margaret Cancer Center, 610 University Avenue, M5G 2M9, Toronto, Canada.
C Jane McGlade§Cell Biology, The Hospital For Sick Children, 686 Bay Street, Toronto, M5G 0A4, Canada; ¶The Arthur and Sonia Labatt Brain Tumour Research Centre, The Hospital For Sick Children, 686 Bay Street, Toronto, M5G 0A4, Canada; ‖Medical Biophysics, University of Toronto, Medical Science Building, Room 4386, 1 King's College Circle, Toronto, ON M5S 1A8, Canada;
Michael F MoranFrom the ‡Molecular Structure and Function, The Hospital For Sick Children, 686 Bay Street, Toronto, M5G 0A4, Canada; ‡‡Departments of Molecular Genetics, Medical Science Building, Room 4386, 1 King's College Circle, Toronto, ON M5S 1A8, Canada; **The Princess Margaret Cancer Center, 610 University Avenue, M5G 2M9, Toronto, Canada m.moran@utoronto.ca.
Hospital for Sick Children · CABrain Tumour Research · GBCanada Research Chairs · CAPrincess Margaret Cancer Centre · CAUniversity of New Brunswick · CAUniversity of Toronto · CA

Funding

Canadian Institutes of Health Research MOP106507
6 · The paper itself

Abstract

Src homology 2 (SH2) domains are modular protein structures that bind phosphotyrosine (pY)-containing polypeptides and regulate cellular functions through protein-protein interactions. Proteomics analysis showed that the SH2 domains of Src family kinases are themselves tyrosine phosphorylated in blood system cancers, including acute myeloid leukemia, chronic lymphocytic leukemia, and multiple myeloma. Using the Src family kinase Lyn SH2 domain as a model, we found that phosphorylation at the conserved SH2 domain residue Y(194) impacts the affinity and specificity of SH2 domain binding to pY-containing peptides and proteins. Analysis of the Lyn SH2 domain crystal structure supports a model wherein phosphorylation of Y(194) on the EF loop modulates the binding pocket that engages amino acid side chains at the pY+2/+3 position. These data indicate another level of regulation wherein SH2-mediated protein-protein interactions are modulated by SH2 kinases and phosphatases.

Indexed as

Amino Acid SequenceBinding SitesCell Line, TumorConserved SequenceCrystallography, X-RayHumansLeukemia, Lymphocytic, Chronic, B-CellLeukemia, Myeloid, AcuteModels, MolecularMultiple MyelomaPhosphotyrosineProtein Structure, SecondaryProteomicssrc-Family Kinasessrc Homology DomainsSubstrate SpecificityPhosphotyrosinesrc-Family Kinases

Identifiers

PMID25587033
PMCPMC4349988
OpenAlexW2159186230

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.