The atypical protein kinase Cs. Functional specificity mediated by specific protein adapters.

TitleThe atypical protein kinase Cs. Functional specificity mediated by specific protein adapters.
Publication TypeJournal Article
Year of Publication2000
AuthorsMoscat J, Diaz-Meco MT
JournalEMBO Rep
Volume1
Issue5
Pagination399-403
Date Published2000 Nov
ISSN1469-221X
KeywordsAmino Acid Sequence, Animals, Apoptosis Regulatory Proteins, Carrier Proteins, Humans, Intracellular Signaling Peptides and Proteins, Models, Biological, Molecular Sequence Data, Protein Binding, Protein Kinase C, Protein Structure, Tertiary, Sequence Homology, Amino Acid, Signal Transduction
Abstract

Since its discovery more than 10 years ago, the atypical PKC (aPKC) subfamily has attracted great interest. A number of reports have shown that the kinases of this subfamily play critical roles in signaling pathways that control cell growth, differentiation and survival. Recently, several investigators have identified a number of aPKC-interacting proteins whose characterization is helping to unravel the mechanisms of action and functions of these kinases. These interactors include p62, Par-6, MEK5 and Par-4. The details of how these adapters serve to link the aPKCs to different receptor signaling pathways and substrates in response to specific stimuli are crucial not only for developing an understanding of the roles and functions of the aPKCs themselves, but also for more generally establishing a view of how specificity in signal transduction is achieved.

DOI10.1093/embo-reports/kvd098
Alternate JournalEMBO Rep
PubMed ID11258478
PubMed Central IDPMC1083770
Related Faculty: 
Jorge Moscat, Ph.D. Maria Diaz-Meco Conde, Ph.D.

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