ArticleJournal of molecular biology2013
Substrate recognition of PLCγ1 via a specific docking surface on Itk.
Article in Journal of molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 21 citations in OpenAlex.
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- Purification and characterization of full-length monomeric TEC family kinase, ITK.Protein expression and purification · 2025Article
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- The Conformational State of the BTK Substrate PLCγ Contributes to Ibrutinib Resistance.Journal of molecular biology · 2022Article
- Reining in BTK: Interdomain Interactions and Their Importance in the Regulatory Control of BTK.Frontiers in cell and developmental biology · 2021Review
- Mesenchymal stem cells from bone marrow regulate invasion and drug resistance of multiple myeloma cells by secreting chemokine CXCL13.Bosnian journal of basic medical sciences · 2020Article
- Lipid-targeting pleckstrin homology domain turns its autoinhibitory face toward the TEC kinases.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Scaffold Protein SLP-76 Primes PLCγ1 for Activation by ITK-Mediated Phosphorylation.Journal of molecular biology · 2015Article
- Identification of new members of the MAPK gene family in plants shows diverse conserved domains and novel activation loop variants.BMC genomics · 2015Article
- A selective NMR probe to monitor the conformational transition from inactive to active kinase.ACS chemical biology · 2015Article
- A conserved isoleucine maintains the inactive state of Bruton's tyrosine kinase.Journal of molecular biology · 2014Article
- The autoinhibitory C-terminal SH2 domain of phospholipase C-γ2 stabilizes B cell receptor signalosome assembly.Science signaling · 2014Article
- Activation loop dynamics determine the different catalytic efficiencies of B cell- and T cell-specific tec kinases.Science signaling · 2013Article
- Partial defects of T-cell development associated with poor T-cell function.The Journal of allergy and clinical immunology · 2013Review
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4 authors at 1 institution in 1 country.
Funding
Abstract
Itk (interleukin-2 inducible T cell kinase) is a non-receptor protein tyrosine kinase expressed primarily in T cells. Itk catalyzes phosphorylation on tyrosine residues within a number of its natural substrates, including the well-characterized Y783 of PLCγ1. However, the molecular mechanisms Itk exploits to recognize its substrates are not completely understood. We have previously identified a specific docking interaction between the kinase domain of Itk and the C-terminal Src homology 2 (SH2C) domain of PLCγ1 that promotes substrate specificity for this enzyme/substrate pair. In the current study, we identify and map the interaction surface on the Itk kinase domain as an acidic patch centered on the G helix. Mutation of the residues on and adjacent to the G helix within the Itk kinase domain impairs the catalytic efficacy of PLCγ1 substrate phosphorylation by specifically altering the protein-protein interaction interface and not the inherent catalytic activity of Itk. NMR titration experiments using a Btk (Bruton's tyrosine kinase) kinase domain as a surrogate for the Itk kinase domain provide further support for an Itk/PLCγ1 SH2C interaction surrounding the G helix of the kinase domain. The work presented here provides structural insight into how the Itk kinase uses the G helix to single out Y783 of PLCγ1 for specific phosphorylation. Comparing these results to other well-characterized kinase/substrate systems suggests that the G helix is a general structural feature used by kinases for substrate recognition during signaling.
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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.