Journal
PROGRESS IN BIOPHYSICS & MOLECULAR BIOLOGY
Volume 98, Issue 2-3, Pages 238-250Publisher
PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.pbiomolbio.2009.01.007
Keywords
Protein phosphatase 2A; L-type Ca2+-channel; Sarcomeric protein phosphorylation; Ryanodine receptor
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Funding
- NIH National Heart Lung and Blood Institute
- NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [R01HL064035, R01HL022231, P01HL062426] Funding Source: NIH RePORTER
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Cardiac excitation and contraction are regulated by a variety of signaling molecules. Central to the regulatory scheme are protein kinases and phosphatases that carry out reversible phosphorylation of different effectors. The process of beta-adrenergic stimulation mediated by cAMP dependent protein kinase (PKA) forms a well-known pathway considered as the most significant Control mechanism in excitation and contraction as well as many other regulatory mechanisms in Cardiac function. However, although dephosphorylation pathways are critical to these regulatory processes, signaling to phosphatases is relatively poorly understood. Emerging evidence indicates that regulation of phosphatases, which dampen the effect of beta-adrenergic stimulation, is also important. We review here functional studies of p21 activated kinase-1 (Pak1) and its potential role as all upstream signal for protein phosphatase PP2A in the heart. Pak1 is a serine/threonine protein kinase directly activated by the small GTPases Cdc42 and Rac1. Pak1 is highly expressed in different re.-ions of the heart and modulates the activities of ion channels, sarcomeric proteins, and other phosphoproteins through up-regulation of PP2A activity. Coordination of Pak1 and PP2A activities is not only potentially involved in regulation of normal cardiac function, but is likely to be important in patho-physiological conditions. (C) 2009 Elsevier Ltd. All rights reserved.
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