PRKCQ
From Wikipedia, the free encyclopedia
Protein kinase C, theta, also known as PRKCQ, is a human gene.
Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that can be activated by calcium and the second messenger diacylglycerol. PKC family members phosphorylate a wide variety of protein targets and are known to be involved in diverse cellular signaling pathways. PKC family members also serve as major receptors for phorbol esters, a class of tumor promoters. Each member of the PKC family has a specific expression profile and is believed to play a distinct role. The protein encoded by this gene is one of the PKC family members. It is a calcium-independent and phospholipid-dependent protein kinase. This kinase is important for T-cell activation. It is required for the activation of the transcription factors NF-kappaB and AP-1, and may link the T cell receptor (TCR) signaling complex to the activation of the transcription factors.[1]
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- Chang JD, Xu Y, Raychowdhury MK, Ware JA (1993). "Molecular cloning and expression of a cDNA encoding a novel isoenzyme of protein kinase C (nPKC). A new member of the nPKC family expressed in skeletal muscle, megakaryoblastic cells, and platelets.". J. Biol. Chem. 268 (19): 14208–14. PMID 7686153.
- Erdel M, Baier-Bitterlich G, Duba C, et al. (1995). "Mapping of the human protein kinase C-theta (PRKCQ) gene locus to the short arm of chromosome 10 (10p15) by FISH.". Genomics 25 (2): 595–7. PMID 7790001.
- Ward NE, Gravitt KR, O'Brian CA (1995). "Inhibition of protein kinase C by a synthetic peptide corresponding to cytoplasmic domain residues 828-848 of the human immunodeficiency virus type 1 envelope glycoprotein.". Cancer Lett. 88 (1): 37–40. PMID 7850771.
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- Baier G, Telford D, Giampa L, et al. (1993). "Molecular cloning and characterization of PKC theta, a novel member of the protein kinase C (PKC) gene family expressed predominantly in hematopoietic cells.". J. Biol. Chem. 268 (7): 4997–5004. PMID 8444877.
- Parada NA, Cruikshank WW, Danis HL, et al. (1996). "IL-16- and other CD4 ligand-induced migration is dependent upon protein kinase C.". Cell. Immunol. 168 (1): 100–6. doi: . PMID 8599832.
- Conant K, Ma M, Nath A, Major EO (1996). "Extracellular human immunodeficiency virus type 1 Tat protein is associated with an increase in both NF-kappa B binding and protein kinase C activity in primary human astrocytes.". J. Virol. 70 (3): 1384–9. PMID 8627654.
- Smith BL, Krushelnycky BW, Mochly-Rosen D, Berg P (1996). "The HIV nef protein associates with protein kinase C theta.". J. Biol. Chem. 271 (28): 16753–7. PMID 8663223.
- Meller N, Liu YC, Collins TL, et al. (1996). "Direct interaction between protein kinase C theta (PKC theta) and 14-3-3 tau in T cells: 14-3-3 overexpression results in inhibition of PKC theta translocation and function.". Mol. Cell. Biol. 16 (10): 5782–91. PMID 8816492.
- Holmes AM (1996). "In vitro phosphorylation of human immunodeficiency virus type 1 Tat protein by protein kinase C: evidence for the phosphorylation of amino acid residue serine-46.". Arch. Biochem. Biophys. 335 (1): 8–12. doi: . PMID 8914829.
- Monks CR, Kupfer H, Tamir I, et al. (1997). "Selective modulation of protein kinase C-theta during T-cell activation.". Nature 385 (6611): 83–6. doi: . PMID 8985252.
- Datta R, Kojima H, Yoshida K, Kufe D (1997). "Caspase-3-mediated cleavage of protein kinase C theta in induction of apoptosis.". J. Biol. Chem. 272 (33): 20317–20. PMID 9252332.