Figure 2


Figure 2: Domain structures of classical, novel, and atypical protein kinase C (PKC). The figure shows a comparison of the protein architecture of the various subgroups of the PKC subfamily. All PKC regulatory domains have a pseudosubstrate domain (shown in green). Conventional and novel PKC contain C1 domain which mediate binding to diacylglycerol (DAG) and phorbol 12-myristate 13-acetate (PMA) and C2 domain which has a function as calcium-dependent phospholipid binding in the case of conventional PKC and a serine/threonine-kinase domain. Novel PKC C2 domains do not bind calcium. The atypical PKC, which lack the C2 region, are not activated by calcium, DAG, or PMA, but their activation depends on phosphatidylserine and cis-unsaturated fatty acids.

Figure 2: Domain structures of classical, novel, and atypical protein kinase C (PKC). The figure shows a comparison of the protein architecture of the various subgroups of the PKC subfamily. All PKC regulatory domains have a pseudosubstrate domain (shown in green). Conventional and novel PKC contain C1 domain which mediate binding to diacylglycerol (DAG) and phorbol 12-myristate 13-acetate (PMA) and C2 domain which has a function as calcium-dependent phospholipid binding in the case of conventional PKC and a serine/threonine-kinase domain. Novel PKC C2 domains do not bind calcium. The atypical PKC, which lack the C2 region, are not activated by calcium, DAG, or PMA, but their activation depends on phosphatidylserine and cis-unsaturated fatty acids.