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In cell biology, protein kinase C, commonly abbreviated to PKC (EC 2.7.11.13), is a family of protein kinase enzymes that are involved in controlling the function of other proteins through the phosphorylation of hydroxyl groups of serine and threonine amino acid residues on these proteins, or a member of this family.
18750 Ensembl ENSG00000154229 ENSMUSG00000050965 UniProt P17252 P20444 RefSeq (mRNA) NM_002737 NM_011101 RefSeq (protein) NP_002728 NP_035231 Location (UCSC) Chr 17: 66.3 – 66.81 Mb Chr 11: 107.82 – 108.23 Mb PubMed search Wikidata View/Edit Human View/Edit Mouse Protein kinase C alpha (PKCα) is an enzyme that in humans is encoded by the PRKCA gene. Function Protein kinase C (PKC) is a ...
PKC-zeta has an N-terminal regulatory domain, followed by a hinge region and a C-terminal catalytic domain. Second messengers stimulate PKCs by binding to the regulatory domain, translocating the enzyme from cytosol to membrane, and producing a conformational change that removes auto-inhibition of the PKC catalytic protein kinase activity.
[4] [44] [45] [46] One example of a protein that binds to adaptor proteins and become activated is PLC that is very important in the lymphocyte signal pathways. PLC is responsible for PKC activation, via DAG and Ca 2+, which leads to phosphorylation of CARMA1 molecule, and formation of CBM complex.
Since smooth muscle does not contain a troponin complex, as striated muscle does, this mechanism is the main pathway for regulating smooth muscle contraction. Reducing intracellular calcium concentration inactivates MLCK but does not stop smooth muscle contraction since the myosin light chain has been physically modified through phosphorylation ...
Protein kinase C theta (PKC-θ) is an enzyme that in humans is encoded by the PRKCQ gene. [5] PKC-θ, a member of serine/threonine kinases, is mainly expressed in hematopoietic cells [5] with high levels in platelets and T lymphocytes, where plays a role in signal transduction. Different subpopulations of T cells vary in their requirements of ...
The structure of PDPK1 can be divided into two domains; the kinase or catalytic domain and the PH domain.The PH domain functions mainly in the interaction of PDPK1 with phosphatidylinositol (3,4)-bisphosphate and phosphatidylinositol (3,4,5)-trisphosphate which is important in localization and activation of some of membrane associated PDPK1's substrates including AKT.
Protein kinase C gamma type is an enzyme that in humans is encoded by the PRKCG gene. [ 5 ] [ 6 ] Protein kinase C (PKC) is a family of serine- and threonine-specific protein kinases that can be activated by calcium and second messenger diacylglycerol.