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Protein kinase C? C2 domain is a phosphotyrosine binding module that plays a key role in its activation.

ABSTRACT: Protein kinase C? (PKC?) is a novel PKC that plays a key role in T lymphocyte activation. To understand how PKC? 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 PKC? with high affinity and activates the enzyme activity of the intact protein. The Tyr(P) peptide also binds the C2 domain of PKC? tightly, but no enzyme activation was observed with PKC?. Mutations of PKC?-C2 residues involved in Tyr(P) binding abrogated the enzyme activation and association of PKC? with Tyr-phosphorylated full-length CDCP1 and severely inhibited the T cell receptor/CD28-mediated activation of a PKC?-dependent reporter gene in T cells. Collectively, these studies establish the C2 domain of PKC? as a Tyr(P)-binding domain and suggest that the domain may play a major role in PKC? activation via its Tyr(P) binding.

SUBMITTER: Stahelin RV

PROVIDER: S-EPMC3436300 | biostudies-literature | 2012 Aug

REPOSITORIES: biostudies-literature

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Protein kinase Cθ C2 domain is a phosphotyrosine binding module that plays a key role in its activation.

Stahelin Robert V RV Kong Kok-Fai KF Raha Sumita S Tian Wen W Melowic Heather R HR Ward Katherine E KE Murray Diana D Altman Amnon A Cho Wonhwa W

The Journal of biological chemistry 20120711 36

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 activa ...[more]

PMID: 22787157

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Project description:Temperature is considered one of the critical factors directly influencing grapevine during the three primary growth and development stages: sprout, flowering, and fruit-coloring, which is strongly correlated to the yield and quality of the grape. The grapevine is frequently exposed to high-temperature conditions that are detrimental to growth. However, the mechanisms of the heat stress response and adaptation in grapevine are not adequately studied. The Arabidopsis copine gene AtBON1 encodes a highly conserved protein containing two C2 domains at the amino terminus, participation in cell death regulation and defense responses. Previously, we showed that a BON1 association protein from the grapevine, VvBAP1, plays a positive role in cold tolerance. Similarly, the involvement of VvBAP1 in the resistance to heat stress was also found in the present study. The results indicated VvBAP1 was significantly induced by high temperature, and the elevated expression of VvBAP1 was significantly higher in the resistant cultivars than the sensitive cultivars under heat stress. Seed germination and phenotypic analysis results indicated that overexpression of VvBAP1 improved Arabidopsis thermoresistance. Compared with the wild type, the chlorophyll content and net photosynthetic rate in VvBAP1 overexpressing Arabidopsis plants were markedly increased under heat stress. At high temperatures, overexpression of VvBAP1 also enhanced antioxidant enzyme activity as well as their corresponding gene transcription levels, to reduce the accumulation of reactive oxygen species and lipid peroxidation. Besides, the transcriptional activities of HSP70, HSP101, HSFA2, and HSFB1 in VvBAP1 overexpressing Arabidopsis plants were significantly up-regulated compare to the wild type. In summary, we propose that VvBAP1 may play a potential important role in enhanced grapevine thermoresistance, primarily through the enhancement of antioxidant enzyme activity and promoted heat stress response genes expression.

Dataset Information

Protein kinase C? C2 domain is a phosphotyrosine binding module that plays a key role in its activation.

Publications

Protein kinase Cθ C2 domain is a phosphotyrosine binding module that plays a key role in its activation.

Similar Datasets

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