High impact information on Pkcdelta

• Expression of cDNA constructs and microinjection of PLC or antibodies against it clearly establish a role for PtdIns signaling distinct from its role in calcium mobilization and protein kinase C activation [1].
• We showed previously that protein kinase C, which is required to maintain cell integrity, negatively regulates cell fusion (Philips, J., and I. Herskowitz. 1997. J. Cell Biol. 138:961-974) [2].
• The phosphorylation state of cp20, a low molecular weight GTP-binding protein that is a high-affinity substrate for protein kinase C, was previously shown to change after associative conditioning of molluscs and mammals and to induce many of the biophysical and structural modifications that accompany memory retention [3].
• We suggest that light or phorbol ester activates a protein kinase C and results in a sustained or excessive phosphorylation of proteins in the rdgB mutant, leading to photoreceptor degeneration [4].
• However, the modes of action of Munc-18 and PKC in vesicle transport have not been clarified [5].

Biological context of Pkcdelta

• Therefore, the phosphorylation by PKC may play a physiological role in the regulation [6].
• During a large-scale screen of a human fetal brain cDNA library, a novel human gene GNB2L1 encoding a novel RACK (receptor of activated protein kinase C) protein was isolated and sequenced [7].
• On the other hand, protein kinase C (PKC) stimulates Ca2+-dependent exocytosis in various types of secretory cells [5].
• Protein kinase Mzeta (PKMzeta), an atypical protein kinase C (PKC) isoform, plays a key role in the maintenance of long-term potentiation (LTP), a persistent enhancement of AMPA receptor-mediated synaptic transmission, as well as in the persistence of memory in Drosophila [8].
• Inhibition of PKC activity by protein kinase inhibitors blocked USP phosphorylation, resulting in inhibition of 20E-induced gene expression at both transcriptional and translational levels [9].

Anatomical context of Pkcdelta

• Here, we show that recombinant Munc-18 is phosphorylated by conventional PKC in a Ca2+- and phospholipid-dependent manner in a cell-free system [5].
• We found that PKMzeta accumulated in neurofibrillary tangles (NFTs), whereas conventional and novel PKC isoforms did not [8].
• The Ca2+-dependent protein kinase C (PKC) isoform PKCalpha plays a crucial role in initiating endothelial cell contraction and disassembly of VE-cadherin junctions [10].
• PKC-mediated USP phosphorylation is required for 20E-induced gene expression in the salivary glands of Drosophila melanogaster [9].

Associations of Pkcdelta with chemical compounds

• Unique structural elements of p170 include C-terminal sequences strikingly similar to the phosphoinositide-binding C2 domain of protein kinase C isoforms, synaptotagmins, and other proteins [11].
• Synaptotagmin contains two domains that are homologous to the calcium ion (Ca(2+))-binding C2 domain of protein kinase C. The two C2 domains of synaptotagmin have broadly differing ligand-binding properties [12].
• ETA receptor subtypes activate downstream effectors, such as protein kinase C, protein tyrosine kinases of the src gene family, and mitogen-activated protein kinases [13].
• Interestingly, the C-terminal tail in ANXs I, II and V were previously confirmed as a binding region for protein kinase C. Thus generation of the three ANX IX isoforms in the silkworm, that are different from other ANXs, may have a functional significance other than binding to Ca(2+) [14].

Analytical, diagnostic and therapeutic context of Pkcdelta

• The gene was deduced to code for a protein kinase C (PKC) homologue by molecular cloning [15].
• Animal models in the study of protein kinase C isozymes [16].

References