Rationally designed peptide regulators of protein kinase C

Eric N. Churchill, Nir Qvit, Daria Mochly-Rosen

Research output: Contribution to journalReview articlepeer-review

88 Scopus citations

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.

Original languageEnglish
Pages (from-to)25-33
Number of pages9
JournalTrends in Endocrinology and Metabolism
Volume20
Issue number1
DOIs
StatePublished - Jan 2009
Externally publishedYes

Bibliographical note

Funding Information:
D.M.-R. is the founder of KAI Pharmaceuticals, a company that plans to bring PKC regulators to the clinic. However, none of the work in her lab is supported by the company.

Funding

D.M.-R. is the founder of KAI Pharmaceuticals, a company that plans to bring PKC regulators to the clinic. However, none of the work in her lab is supported by the company.

FundersFunder number
National Institutes of HealthHL76670, HL52141
National Institute on Alcohol Abuse and AlcoholismR01AA011147

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