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• W2016184567 endingPage "33" @default.
• W2016184567 startingPage "25" @default.
• W2016184567 abstract "Protein–protein interactions sequester enzymes close to their substrates. Protein kinase C (PKC) is one example of a ubiquitous signaling molecule with effects that are dependent upon localization. Short peptides derived from interaction sites between each PKC isozyme and its receptor for activated C kinase act as highly specific inhibitors and have become available as selective drugs in basic research and animal models of human diseases, such as myocardial infarction and hyperglycemia. Whereas the earlier inhibitory peptides are highly specific, we believe that peptides targeting additional interactions between PKC and selective substrates will generate even more selective tools that regulate different functions of individual isozymes. Here, we discuss the methodologies and applications for identifying selective regulators of PKC. Protein–protein interactions sequester enzymes close to their substrates. Protein kinase C (PKC) is one example of a ubiquitous signaling molecule with effects that are dependent upon localization. Short peptides derived from interaction sites between each PKC isozyme and its receptor for activated C kinase act as highly specific inhibitors and have become available as selective drugs in basic research and animal models of human diseases, such as myocardial infarction and hyperglycemia. Whereas the earlier inhibitory peptides are highly specific, we believe that peptides targeting additional interactions between PKC and selective substrates will generate even more selective tools that regulate different functions of individual isozymes. Here, we discuss the methodologies and applications for identifying selective regulators of PKC. a motif composed of eight β strands creating two flat sheets connected with a short helix ‘hinge’. The C2 domain can bind 2–3 calcium ions, thus increasing interaction with negatively charged phospholipids (i.e. phosphatidylserine) in membranes. Calcium and lipid binding is a common feature of C2 domains. a family of enzymes responsible for the conversion of arachidonic acid to prostaglandins. They are the targets of non-steroidal anti-inflammatory agents, which can reduce symptoms of inflammation and pain. a second messenger signaling molecule, which anchors PKC to membranes, resulting in its activation. It is generated from the phospholipase-C2-dependent cleavage of phosphatidyl inositol bisphosphate and is mimicked by phorbol esters, such as phorbol 12-myristate 13-acetate. short peptides (6–10 amino acids) that either disrupt or enhance PKC isozyme binding to their respective RACKs. short peptides that can regulate PKC subdomain interactions with target substrates independent of RACK binding, therefore conferring even greater specificity. homologous enzymes that are products of different genes or alternatively spliced mRNA of the same gene and, thus, belong to the same family of enzymes. as applied here, constraints introduced within a peptide substantially reduce the theoretically possible conformational states of a linear peptide and are powerful tools for studying interactions in biological systems. Local constraints can be enforced by using unnatural or natural amino acids, and global constraints can be induced by cyclization of the peptide. computer simulation that enables modeling of the three-dimensional position of atoms within a molecule to understand dynamic changes in their structure and interactions. an enzyme that catalyzes the hydrolysis of phospholipids such as phosphatidyl inositol bisphosphate to diacylglycerol and the remaining lipid head group, inositol trisphosphate. Similar to PKC, phospholipase C contains a C2 domain, which enables its anchoring to different proteins. an enzyme that catalyzes the hydrolysis of phosphatidylcholine to phosphatidic acid that can be further converted to diacylglycerol. Similar to PKC, phospholipase D contains a C2 domain, enabling its anchoring to different proteins. regions on PKC that are homologous to the RACK protein. The pseudo-RACK site in PKC binds to the RACK-binding site in an intramolecular interaction, which stabilizes the isozyme in its inactive state. Peptides corresponding to this sequence interfere with the intramolecular interaction and, thus, activate PKC. a tumor promoter that mimics diacylglycerol binding to and activation of PKC. proteins in the cellular particulate fraction that bind activated PKC in a saturable and specific manner but are themselves not substrates of PKC. a protein involved in synaptic vesicle discharge. The protein has no catalytic activity, but it contains two repeats of the C2 domain and, like PKC, these domains enable its anchoring to membranes." @default.
• W2016184567 created "2016-06-24" @default.
• W2016184567 creator A5001021574 @default.
• W2016184567 creator A5019697239 @default.
• W2016184567 creator A5039639608 @default.
• W2016184567 date "2009-01-01" @default.
• W2016184567 modified "2023-10-14" @default.
• W2016184567 title "Rationally designed peptide regulators of protein kinase C" @default.
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