What is PKC theta?
Protein kinase C theta (PKC-θ) is an enzyme that in humans is encoded by the PRKCQ gene. PKC-θ, a member of serine/threonine kinases, is mainly expressed in hematopoietic cells with high levels in platelets and T lymphocytes, where plays a role in signal transduction.
Is cell division controlled by PKC?
Although PKCs can regulate all stages of the cell cycle, they appear to predominantly affect G0/G1 and G2. Analysis of PKC signaling in T cells has largely focused on its roles in T cell activation; thus, observed cell cycle effects are mainly positive.
Which molecule activates PKC?
PKC enzymes in turn are activated by signals such as increases in the concentration of diacylglycerol (DAG) or calcium ions (Ca2+). Hence PKC enzymes play important roles in several signal transduction cascades.
What is PKC responsible for?
Protein kinase C (PKC) family members regulate numerous cellular responses including gene expression, protein secretion, cell proliferation, and the inflammatory response. The basic protein structure includes an N-terminal regulatory region connected to a C-terminal kinase domain by a hinge region.
What does PKC do in muscle?
Protein kinase M induces relaxation of demembranated smooth muscle fibers contracted at submaximal Ca2+ concentrations. We suggest that protein kinase C plays two distinct roles in regulating smooth muscle contractility.
What is Pkcθ?
Protein kinase C-theta (PKCθ) is a member of the novel, Ca2+-independent PKC subfamily, which plays an important and non-redundant role in several aspects of T cell biology. Biochemical and genetic approaches revealed that PKCθ is required for the activation of mature T cells as well as for their survival.
What is the role of PKC?
Protein Kinase-C (also known as PKC) is a family of protein kinase enzymes that are involved in controlling the function of other proteins via the phosphorylation of hydroxyl groups of serine and threonine amino acid residues.
What is PKC signaling?
Protein kinase C (PKC) form a key family of enzymes involved in signalling pathways that specifically phosphorylates substrates at serine/threonine residues. Phosphorylation by PKC is important in regulating a variety of cellular events such as cell proliferation and the regulation of gene expression.
How does PKC cause contraction?
PKC may also phosphorylate the actin-binding protein calponin, and thereby reverses its inhibition of actin-activated myosin ATPase, allows more actin to interact with myosin, and increases VSM contraction (Figure 1.1) [2].