ArticleThe Journal of biological chemistry2012
Protein kinase Cθ C2 domain is a phosphotyrosine binding module that plays a key role in its activation.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 26 citations in OpenAlex.
- Association of PRKCQ variants with breast cancer susceptibility and clinicopathological features.BMC cancer · 2025Article
- Phosphotyrosine-dependent interaction between the kinases PKCθ and Zap70 promotes proximal TCR signaling.Science signaling · 2019Article
- Regulation of inside-out β1-integrin activation by CDCP1.Oncogene · 2018Article
- Chemical proteomic map of dimethyl fumarate-sensitive cysteines in primary human T cells.Science signaling · 2016Article
- Spatio-Temporal Regulation of PKC Isoforms Imparts Signaling Specificity.Frontiers in immunology · 2016Review
- Signaling in Effector Lymphocytes: Insights toward Safer Immunotherapy.Frontiers in immunology · 2016Review
- Dynamics and Membrane Interactions of Protein Kinase C.Biochemistry · 2015Review
- Mechanisms for redox-regulation of protein kinase C.Frontiers in pharmacology · 2015Review
- Intramolecular conformational changes optimize protein kinase C signaling.Chemistry & biology · 2014Article
- Atypical protein kinase Cι as a human oncogene and therapeutic target.Biochemical pharmacology · 2014Review
- From lipid second messengers to molecular motors: microtubule-organizing center reorientation in T cells.Immunological reviews · 2013Review
- In and out of the bull's eye: protein kinase Cs in the immunological synapse.Trends in immunology · 2013Review
- Phosphotyrosine recognition domains: the typical, the atypical and the versatile.Cell communication and signaling : CCS · 2012Article
Corrections and comments
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Authors and funding
9 authors at 6 institutions in 2 countries.
Funding
Abstract
Protein kinase Cθ (PKCθ) is a novel PKC that plays a key role in T lymphocyte activation. To understand how PKCθ is regulated in T cells, we investigated the properties of its N-terminal C2 domain that functions as an autoinhibitory domain. Our measurements show that a Tyr(P)-containing peptide derived from CDCP1 binds the C2 domain of PKCθ with high affinity and activates the enzyme activity of the intact protein. The Tyr(P) peptide also binds the C2 domain of PKCδ tightly, but no enzyme activation was observed with PKCδ. Mutations of PKCθ-C2 residues involved in Tyr(P) binding abrogated the enzyme activation and association of PKCθ with Tyr-phosphorylated full-length CDCP1 and severely inhibited the T cell receptor/CD28-mediated activation of a PKCθ-dependent reporter gene in T cells. Collectively, these studies establish the C2 domain of PKCθ as a Tyr(P)-binding domain and suggest that the domain may play a major role in PKCθ activation via its Tyr(P) binding.
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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.