title: Protein kinase C (PKC) isoforms in Drosophila.
abstract: Six protein kinase C (PKC) genes are present in Drosophila, comprising two classical PKCs (PKC53E and eye-PKC), two novel PKCs (PKC98E and PKCdelta), an atypical PKC (DaPKC), and a PKC-related kinase. Loss of function alleles affecting DaPKC and eye-PKC are available and their mutant phenotypes have been characterized. DaPKC is essential for early embryonic development because it regulates cell polarity and asymmetric cell division. Eye-PKC plays a role in the regulation of visual signaling, a G-protein coupled phospholipase Cbeta-mediated cascade. Both eye-PKC and DaPKC are differentially localized through tethering to multimolecular complexes. DaPKC interacts with partitioning-defective 3 (Par-3) and Par-6 proteins, which contain PDZ (PSD95, DLG, ZO-1) domains. Similarly, eye-PKC is anchored to a PDZ domain containing scaffolding protein INAD. Characterization of these two PKCs in Drosophila revealed a universal mechanism by which PKC is tethered to specific protein complexes for participation in distinct signal transduction processes.
mesh_terms: D000818:Animals; D016764:Cell Polarity / Q000502:physiology; D030541:Databases, Genetic; D004330:Drosophila / Q000201:enzymology* / Q000235:genetics / Q000502:physiology; D029721:Drosophila Proteins / Q000737:chemistry / Q000502:physiology*; D005136:Eye Proteins / Q000737:chemistry / Q000502:physiology; D006801:Humans; D019476:Insect Proteins / Q000737:chemistry / Q000502:physiology*; D007527:Isoenzymes / Q000737:chemistry / Q000502:physiology; D011493:Protein Kinase C / Q000737:chemistry / Q000502:physiology*; D017434:Protein Structure, Tertiary / Q000502:physiology; D015398:Signal Transduction; D014785:Vision, Ocular / Q000502:physiology
chemical_list: D029721:Drosophila Proteins; D005136:Eye Proteins; D019476:Insect Proteins; D007527:Isoenzymes; D011493:Protein Kinase C