ArticleNature communications2021
Structural and functional analysis of target recognition by the lymphocyte adaptor protein LNK.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
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Who cites it
12 citing papers in PubMed, 14 citations in OpenAlex.
- Intratumoral B cell and interferon signatures in newly diagnosed glioblastoma are associated with longer survival in patients treated with SurVaxM.Cancer immunology, immunotherapy : CII · 2025Trial
- Post-translational Modifications in Proteins: Prediction Methods, Biological Functions, and Diseases.MedComm · 2026Review
- Interferon signaling gene expression, and DNA methylation interactions in Sjögren's disease via mendelian randomization.iScience · 2026Article
- Lnk deficiency attenuates the immunosuppressive capacity of MDSCs via ferroptosis to suppress tumor development.Cell death & disease · 2025Article
- The role of LNK in mitigating hypertension: inhibition of vascular smooth muscle proliferation and JAK-STAT pathway.Molecular and cellular biochemistry · 2025Article
- Prognostic and Immunologic Significance of SH2B2 in Colon Adenocarcinoma and its Relationship to Proliferation, Migration, and Invasion.Combinatorial chemistry & high throughput screening · 2025Article
- Rare SH2B3 coding variants in lupus patients impair B cell tolerance and predispose to autoimmunity.The Journal of experimental medicine · 2024Article
- Article
- Modulation of JAK-STAT Signaling by LNK: A Forgotten Oncogenic Pathway in Hormone Receptor-Positive Breast Cancer.International journal of molecular sciences · 2023Review
- Integrative Analysis Reveals the Diverse Effects of 3D Stiffness upon Stem Cell Fate.International journal of molecular sciences · 2023Article
- Biallelic deleterious germlineEJHaem · 2023Article
- The Role of LNK (SH2B3) in the Regulation of JAK-STAT Signalling in Haematopoiesis.Pharmaceuticals (Basel, Switzerland) · 2021Review
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The SH2B family of adaptor proteins, SH2-B, APS, and LNK are key modulators of cellular signalling pathways. Whilst SH2-B and APS have been partially structurally and biochemically characterised, to date there has been no such characterisation of LNK. Here we present two crystal structures of the LNK substrate recognition domain, the SH2 domain, bound to phosphorylated motifs from JAK2 and EPOR, and biochemically define the basis for target recognition. The LNK SH2 domain adopts a canonical SH2 domain fold with an additional N-terminal helix. Targeted analysis of binding to phosphosites in signalling pathways indicated that specificity is conferred by amino acids one- and three-residues downstream of the phosphotyrosine. Several mutations in LNK showed impaired target binding in vitro and a reduced ability to inhibit signalling, allowing an understanding of the molecular basis of LNK dysfunction in variants identified in patients with myeloproliferative disease.
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