The role of protein kinase C-mediated phosphorylation of sarcomeric proteins in the heart-detrimental or beneficial?

Viola Kooij, Ger J.M. Stienen, Jolanda van der Velden

Research output: Contribution to journalReview articleAcademicpeer-review

Abstract

Protein kinase C (PKC) is a family of serine/threonine protein kinases, and alterations have been found in PKC isoform expression and localization in the failing heart. These alterations in PKC activation levels influence the PKC-mediated phosphorylation status of cellular target proteins involved in Ca2+-handling and sarcomeric contraction. The differences observed in the effects due to PKC-mediated phosphorylation may underlie part of the contractile dysfunction observed in the failing heart. It is therefore important to establish the beneficial and detrimental effects of this kinase in the healthy and failing heart. The function of PKC has been studied intensively; however, the complexity of the regulation of this kinase makes the interpretation of the different effects difficult. The main focus of this review is the (patho)physiological impact of phosphorylation of sarcomeric proteins, myosin light chain-2, troponin I and T, desmin, myosin binding protein-C, and titin by PKC.

LanguageEnglish
Pages107-117
Number of pages11
JournalBiophysical Reviews
Volume3
Issue number3
DOIs
Publication statusPublished - 1 Dec 2011

Cite this

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title = "The role of protein kinase C-mediated phosphorylation of sarcomeric proteins in the heart-detrimental or beneficial?",
abstract = "Protein kinase C (PKC) is a family of serine/threonine protein kinases, and alterations have been found in PKC isoform expression and localization in the failing heart. These alterations in PKC activation levels influence the PKC-mediated phosphorylation status of cellular target proteins involved in Ca2+-handling and sarcomeric contraction. The differences observed in the effects due to PKC-mediated phosphorylation may underlie part of the contractile dysfunction observed in the failing heart. It is therefore important to establish the beneficial and detrimental effects of this kinase in the healthy and failing heart. The function of PKC has been studied intensively; however, the complexity of the regulation of this kinase makes the interpretation of the different effects difficult. The main focus of this review is the (patho)physiological impact of phosphorylation of sarcomeric proteins, myosin light chain-2, troponin I and T, desmin, myosin binding protein-C, and titin by PKC.",
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The role of protein kinase C-mediated phosphorylation of sarcomeric proteins in the heart-detrimental or beneficial? / Kooij, Viola; Stienen, Ger J.M.; van der Velden, Jolanda.

In: Biophysical Reviews, Vol. 3, No. 3, 01.12.2011, p. 107-117.

Research output: Contribution to journalReview articleAcademicpeer-review

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T1 - The role of protein kinase C-mediated phosphorylation of sarcomeric proteins in the heart-detrimental or beneficial?

AU - Kooij, Viola

AU - Stienen, Ger J.M.

AU - van der Velden, Jolanda

PY - 2011/12/1

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N2 - Protein kinase C (PKC) is a family of serine/threonine protein kinases, and alterations have been found in PKC isoform expression and localization in the failing heart. These alterations in PKC activation levels influence the PKC-mediated phosphorylation status of cellular target proteins involved in Ca2+-handling and sarcomeric contraction. The differences observed in the effects due to PKC-mediated phosphorylation may underlie part of the contractile dysfunction observed in the failing heart. It is therefore important to establish the beneficial and detrimental effects of this kinase in the healthy and failing heart. The function of PKC has been studied intensively; however, the complexity of the regulation of this kinase makes the interpretation of the different effects difficult. The main focus of this review is the (patho)physiological impact of phosphorylation of sarcomeric proteins, myosin light chain-2, troponin I and T, desmin, myosin binding protein-C, and titin by PKC.

AB - Protein kinase C (PKC) is a family of serine/threonine protein kinases, and alterations have been found in PKC isoform expression and localization in the failing heart. These alterations in PKC activation levels influence the PKC-mediated phosphorylation status of cellular target proteins involved in Ca2+-handling and sarcomeric contraction. The differences observed in the effects due to PKC-mediated phosphorylation may underlie part of the contractile dysfunction observed in the failing heart. It is therefore important to establish the beneficial and detrimental effects of this kinase in the healthy and failing heart. The function of PKC has been studied intensively; however, the complexity of the regulation of this kinase makes the interpretation of the different effects difficult. The main focus of this review is the (patho)physiological impact of phosphorylation of sarcomeric proteins, myosin light chain-2, troponin I and T, desmin, myosin binding protein-C, and titin by PKC.

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KW - Kinase

KW - Phosphorylation

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