ArticleJournal of molecular biology2009
SH2-dependent autophosphorylation within the Tec family kinase Itk.
Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 18 citations in OpenAlex.
- Platelet Membrane Receptors and Signalling Pathways.Handbook of experimental pharmacology · 2026Review
- Regulation of the Tec family of non-receptor tyrosine kinases in cardiovascular disease.Cell death discovery · 2022Review
- Combination Approaches to Target PD-1 Signaling in Cancer.Frontiers in immunology · 2022Review
- Btk SH2-kinase interface is critical for allosteric kinase activation and its targeting inhibits B-cell neoplasms.Nature communications · 2020Article
- Substrate recognition of PLCγ1 via a specific docking surface on Itk.Journal of molecular biology · 2013Article
- A measured approach: determining the PLCγ1 docking site on Itk using a biochemical ruler.Journal of molecular biology · 2013Article
- DEF6, a novel substrate for the Tec kinase ITK, contains a glutamine-rich aggregation-prone region and forms cytoplasmic granules that co-localize with P-bodies.The Journal of biological chemistry · 2012Article
- Rescue of the aggregation prone Itk Pleckstrin Homology domain by two mutations derived from the related kinases, Btk and Tec.Protein science : a publication of the Protein Society · 2012Article
- Two closely spaced tyrosines regulate NFAT signaling in B cells via Syk association with Vav.Molecular and cellular biology · 2011Article
- Controlling the activity of the Tec kinase Itk by mutation of the phenylalanine gatekeeper residue.Biochemistry · 2011Article
- Identification of an allosteric signaling network within Tec family kinases.Journal of molecular biology · 2010Article
- Itk tyrosine kinase substrate docking is mediated by a nonclassical SH2 domain surface of PLCgamma1.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The Tec family kinase, Itk (interleukin-2 tyrosine kinase), undergoes an in cis autophosphorylation on Y180 within its Src homology 3 (SH3) domain. Autophosphorylation of the Itk SH3 domain by the Itk kinase domain is strictly dependent on the presence of the intervening Src homology 2 (SH2) domain. A direct docking interaction between the Itk kinase and SH2 domains brings the Itk SH3 domain into the active site where Y180 is then phosphorylated. We now identify the residues on the surface of the Itk SH2 domain responsible for substrate docking and show that this SH2 surface mediates autophosphorylation in the full-length Itk molecule. The canonical phospholigand binding site on the SH2 domain is not involved in substrate docking, instead the docking site consists of side chains from three loop regions (AB, EF and BG) and part of the betaD strand. These results are extended into Btk (Bruton's tyrosine kinase), a Tec family kinase linked to the B-cell deficiency X-linked agammaglobulinemia (XLA). Our results suggest that some XLA-causing mutations might impair Btk phosphorylation.
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Registered trials
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.