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Articles

Regulation of Cardiac Stress Signaling by Protein Kinase D1

Brooke C. Harrison, Mi-Sung Kim, Eva van Rooij, Craig F. Plato, Philip J. Papst, Rick B. Vega, John A. McAnally, James A. Richardson, Rhonda Bassel-Duby, Eric N. Olson, Timothy A. McKinsey
Brooke C. Harrison
Myogen, Inc., 7575 West 103rd Ave., Westminster, Colorado 80021
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Mi-Sung Kim
Department of Molecular Biology
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Eva van Rooij
Department of Molecular Biology
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Craig F. Plato
Myogen, Inc., 7575 West 103rd Ave., Westminster, Colorado 80021
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Philip J. Papst
Myogen, Inc., 7575 West 103rd Ave., Westminster, Colorado 80021
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Rick B. Vega
Department of Molecular Biology
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John A. McAnally
Department of Molecular Biology
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James A. Richardson
Department of Molecular BiologyDepartment of Pathology, The University of Texas Southwestern Medical Center at Dallas, 5323 Harry Hines Blvd., Dallas, Texas 75390-9148
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Rhonda Bassel-Duby
Department of Molecular Biology
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Eric N. Olson
Department of Molecular Biology
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  • For correspondence: timothy.mckinsey@myogen.com eric.olson@utsouthwestern.edu
Timothy A. McKinsey
Myogen, Inc., 7575 West 103rd Ave., Westminster, Colorado 80021
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  • For correspondence: timothy.mckinsey@myogen.com eric.olson@utsouthwestern.edu
DOI: 10.1128/MCB.26.10.3875-3888.2006
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ABSTRACT

In response to pathological stresses such as hypertension or myocardial infarction, the heart undergoes a remodeling process that is associated with myocyte hypertrophy, myocyte death, and fibrosis. Histone deacetylase 5 (HDAC5) is a transcriptional repressor of cardiac remodeling that is subject to phosphorylation-dependent neutralization in response to stress signaling. Recent studies have suggested a role for protein kinase C (PKC) and its downstream effector, protein kinase D1 (PKD1), in the control of HDAC5 phosphorylation. While PKCs are well-documented regulators of cardiac signaling, the function of PKD1 in heart muscle remains unclear. Here, we demonstrate that PKD1 catalytic activity is stimulated in cardiac myocytes by diverse hypertrophic agonists that signal through G protein-coupled receptors (GPCRs) and Rho GTPases. PKD1 activation in cardiomyocytes occurs through PKC-dependent and -independent mechanisms. In vivo, cardiac PKD1 is activated in multiple rodent models of pathological cardiac remodeling. PKD1 activation correlates with phosphorylation-dependent nuclear export of HDAC5, and reduction of endogenous PKD1 expression with small interfering RNA suppresses HDAC5 shuttling and associated cardiomyocyte growth. Conversely, ectopic overexpression of constitutively active PKD1 in mouse heart leads to dilated cardiomyopathy. These findings support a role for PKD1 in the control of pathological remodeling of the heart via its ability to phosphorylate and neutralize HDAC5.

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Regulation of Cardiac Stress Signaling by Protein Kinase D1
Brooke C. Harrison, Mi-Sung Kim, Eva van Rooij, Craig F. Plato, Philip J. Papst, Rick B. Vega, John A. McAnally, James A. Richardson, Rhonda Bassel-Duby, Eric N. Olson, Timothy A. McKinsey
Molecular and Cellular Biology Apr 2006, 26 (10) 3875-3888; DOI: 10.1128/MCB.26.10.3875-3888.2006

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Regulation of Cardiac Stress Signaling by Protein Kinase D1
Brooke C. Harrison, Mi-Sung Kim, Eva van Rooij, Craig F. Plato, Philip J. Papst, Rick B. Vega, John A. McAnally, James A. Richardson, Rhonda Bassel-Duby, Eric N. Olson, Timothy A. McKinsey
Molecular and Cellular Biology Apr 2006, 26 (10) 3875-3888; DOI: 10.1128/MCB.26.10.3875-3888.2006
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