ArticleProceedings of the National Academy of Sciences of the United States of America1996
Evidence for a role for the phosphotyrosine-binding domain of Shc in interleukin 2 signaling.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 104 citations in OpenAlex.
- Cytokines in Focus: IL-2 and IL-15 in NK Adoptive Cell Cancer Immunotherapy.Immune network · 2025Review
- Guanine nucleotide exchange factor αPIX leads to activation of the Rac 1 GTPase/glycogen phosphorylase pathway in interleukin (IL)-2-stimulated T cells.The Journal of biological chemistry · 2015Article
- IL-15: a central regulator of celiac disease immunopathology.Immunological reviews · 2014Review
- Malignant transformation of CD4+ T lymphocytes mediated by oncogenic kinase NPM/ALK recapitulates IL-2-induced cell signaling and gene expression reprogramming.Journal of immunology (Baltimore, Md. : 1950) · 2013Article
- Rac1 protein regulates glycogen phosphorylase activation and controls interleukin (IL)-2-dependent T cell proliferation.The Journal of biological chemistry · 2012Article
- TCR-mediated Erk activation does not depend on Sos and Grb2 in peripheral human T cells.EMBO reports · 2012Article
- Interleukin-15 regulates proliferation and self-renewal of adult neural stem cells.Molecular biology of the cell · 2011Article
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- Evidence of STAT5-dependent and -independent routes to CD8 memory formation and a preferential role for IL-7 over IL-15 in STAT5 activation.Immunology and cell biology · 2010Article
- p66shc negatively regulates insulin-like growth factor I signal transduction via inhibition of p52shc binding to Src homology 2 domain-containing protein tyrosine phosphatase substrate-1 leading to impaired growth factor receptor-bound protein-2 membrane recruitment.Molecular endocrinology (Baltimore, Md.) · 2008Article
- Interleukin-2 receptor signaling in regulatory T cell development and homeostasis.Immunology letters · 2007Review
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- PIP3 pathway in regulatory T cells and autoimmunity.Immunologic research · 2007Review
- Molecular signatures induced by interleukin-2 on peripheral blood mononuclear cells and T cell subsets.Journal of translational medicine · 2006Article
- Distinct pathways involving the FK506-binding proteins 12 and 12.6 underlie IL-2-versus IL-15-mediated proliferation of T cells.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
- IL-2 negatively regulates IL-7 receptor alpha chain expression in activated T lymphocytes.Proceedings of the National Academy of Sciences of the United States of America · 2002Article
- Signaling via Shc family adapter proteins.Oncogene · 2001Review
- New role for Shc in activation of the phosphatidylinositol 3-kinase/Akt pathway.Molecular and cellular biology · 2000Article
- Hierarchy of protein tyrosine kinases in interleukin-2 (IL-2) signaling: activation of syk depends on Jak3; however, neither Syk nor Lck is required for IL-2-mediated STAT activation.Molecular and cellular biology · 2000Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Stimulation via the T-cell growth factor interleukin 2 (IL-2) leads to tyrosine phosphorylation of Shc, the interaction of Shc with Grb2, and the Ras GTP/GDP exchange factor, mSOS. Shc also coprecipitates with the IL-2 receptor (IL-2R), and therefore, may link IL-2R to Ras activation. We have further characterized the Shc-IL-2R interaction and have made the following observations. (i) Among the two phosphotyrosine-interaction domains present in Shc, the phosphotyrosine-binding (PTB) domain, rather than its SH2 domain, interacts with the tyrosine-phosphorylated IL-2R beta chain. Moreover, the Shc-PTB domain binds a phosphopeptide derived from the IL-2R beta chain (corresponding to residues surrounding Y338, SCFTNQGpYFF) with high affinity. (ii) In vivo, mutant IL-2R beta chains lacking the acidic region of IL-2Rbeta (which contains Y338) fail to phosphorylate Shc. Furthermore, when wild type or mutant Shc proteins that lack the PTB domain were expressed in the IL-2-dependent CTLL-20 cell line, an intact Shc-PTB domain was required for Shc phosphorylation by the IL-2R, which provides further support for a Shc-PTB-IL-2R interaction in vivo. (iii) PTB and SH2 domains of Shc associate with different proteins in IL-2- and T-cell-receptor-stimulated lysates, suggesting that Shc, through the concurrent use of its two different phosphotyrosine-binding domains, could assemble multiple protein complexes. Taken together, our in vivo and in vitro observations suggest that the PTB domain of Shc interacts with Y338 of the IL-2R and provide evidence for a functional role for the Shc-PTB domain in IL-2 signaling.
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