Biochemistry Publications

Title

Protein Kinases and Caspases: Bidirectional Interactions in Apoptosis

Document Type

Article

Publication Date

10-1-2015

Journal

Kinomics: Approaches and Applications

First Page

85

Last Page

114

URL with Digital Object Identifier

10.1002/9783527683031.ch4

Abstract

© 2015 Wiley-VCH Verlag GmbH & Co. KGaA,. All rights reserved. This chapter highlights the prevalence of protein kinase signaling in apoptotic pathways and emphasizes the emergence of global strategies to systematically investigate bidirectional crosstalk between protein kinase phosphorylation and caspase-mediated proteolysis in the propagation of irreversible apoptotic induction. Caspases are classified as cysteine proteases that catalyze irreversible cleavage of peptide bonds C-terminal to aspartic acid residues. The apoptotic role of protein kinases is of interest because posttranslational phosphorylation of both caspases and caspase substrates affects caspase functionality, and conversely, a variety of protein kinases are proteolytically digested by caspases to facilitate or prevent apoptosis. Throughout this chapter, examples have been provided highlighting the complex interactions between protein kinases and caspases that facilitate the progression of apoptosis. The emergence of novel strategies involving proteomics, computational approaches, and techniques designed to monitor the spatial and temporal induction of apoptotic pathways within intact cells offers comprehensive new insights regarding kinase-caspase interactions.

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