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cMyBP-C as a promiscuous substrate: phosphorylation by non-PKA kinases and its potential significance.

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cMyBP-C as a promiscuous substrate: phosphorylation by non-PKA kinases and its potential significance. / Bardswell, Sonya C; Cuello, Friedericke; Kentish, Jonathan C; Avkiran, Metin.

In: J MUSCLE RES CELL M, Vol. 33, No. 1, 1, 2012, p. 53-60.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Bardswell, SC, Cuello, F, Kentish, JC & Avkiran, M 2012, 'cMyBP-C as a promiscuous substrate: phosphorylation by non-PKA kinases and its potential significance.', J MUSCLE RES CELL M, vol. 33, no. 1, 1, pp. 53-60. <http://www.ncbi.nlm.nih.gov/pubmed/22089698?dopt=Citation>

APA

Bardswell, S. C., Cuello, F., Kentish, J. C., & Avkiran, M. (2012). cMyBP-C as a promiscuous substrate: phosphorylation by non-PKA kinases and its potential significance. J MUSCLE RES CELL M, 33(1), 53-60. [1]. http://www.ncbi.nlm.nih.gov/pubmed/22089698?dopt=Citation

Vancouver

Bardswell SC, Cuello F, Kentish JC, Avkiran M. cMyBP-C as a promiscuous substrate: phosphorylation by non-PKA kinases and its potential significance. J MUSCLE RES CELL M. 2012;33(1):53-60. 1.

Bibtex

@article{6db4959bd9ad434f8f22af8bd28c5d40,
title = "cMyBP-C as a promiscuous substrate: phosphorylation by non-PKA kinases and its potential significance.",
abstract = "It is now generally accepted that phosphorylation of cMyBP-C is critically important in maintaining normal cardiac function. Although much of the work to date on phospho-regulation of cMyBP-C has focused on the role of protein kinase A (PKA, also known as cAMP-dependent protein kinase), recent evidence suggests that a number of non-PKA serine/threonine kinases, such as Ca(2+)/calmodulin-dependent protein kinase II, protein kinase C, protein kinase D and the 90-kDa ribosomal S6 kinase are also capable of targeting this key regulatory sarcomeric protein. This article reviews such evidence and proposes a hypothetical role for some of the pertinent signalling pathways in phospho-regulation of cMyBP-C in the setting of heart failure.",
keywords = "Animals, Humans, Binding Sites, Substrate Specificity, Phosphorylation, Calcium/metabolism, *Signal Transduction, Protein Kinase C/*metabolism, Calcium-Calmodulin-Dependent Protein Kinase Type 2/*metabolism, Carrier Proteins/*metabolism, Cyclic AMP-Dependent Protein Kinases/metabolism, Heart Failure/metabolism/pathology, Myofibrils/metabolism, Ribosomal Protein S6 Kinases, 90-kDa/metabolism, Animals, Humans, Binding Sites, Substrate Specificity, Phosphorylation, Calcium/metabolism, *Signal Transduction, Protein Kinase C/*metabolism, Calcium-Calmodulin-Dependent Protein Kinase Type 2/*metabolism, Carrier Proteins/*metabolism, Cyclic AMP-Dependent Protein Kinases/metabolism, Heart Failure/metabolism/pathology, Myofibrils/metabolism, Ribosomal Protein S6 Kinases, 90-kDa/metabolism",
author = "Bardswell, {Sonya C} and Friedericke Cuello and Kentish, {Jonathan C} and Metin Avkiran",
year = "2012",
language = "English",
volume = "33",
pages = "53--60",
journal = "J MUSCLE RES CELL M",
issn = "0142-4319",
publisher = "Springer Netherlands",
number = "1",

}

RIS

TY - JOUR

T1 - cMyBP-C as a promiscuous substrate: phosphorylation by non-PKA kinases and its potential significance.

AU - Bardswell, Sonya C

AU - Cuello, Friedericke

AU - Kentish, Jonathan C

AU - Avkiran, Metin

PY - 2012

Y1 - 2012

N2 - It is now generally accepted that phosphorylation of cMyBP-C is critically important in maintaining normal cardiac function. Although much of the work to date on phospho-regulation of cMyBP-C has focused on the role of protein kinase A (PKA, also known as cAMP-dependent protein kinase), recent evidence suggests that a number of non-PKA serine/threonine kinases, such as Ca(2+)/calmodulin-dependent protein kinase II, protein kinase C, protein kinase D and the 90-kDa ribosomal S6 kinase are also capable of targeting this key regulatory sarcomeric protein. This article reviews such evidence and proposes a hypothetical role for some of the pertinent signalling pathways in phospho-regulation of cMyBP-C in the setting of heart failure.

AB - It is now generally accepted that phosphorylation of cMyBP-C is critically important in maintaining normal cardiac function. Although much of the work to date on phospho-regulation of cMyBP-C has focused on the role of protein kinase A (PKA, also known as cAMP-dependent protein kinase), recent evidence suggests that a number of non-PKA serine/threonine kinases, such as Ca(2+)/calmodulin-dependent protein kinase II, protein kinase C, protein kinase D and the 90-kDa ribosomal S6 kinase are also capable of targeting this key regulatory sarcomeric protein. This article reviews such evidence and proposes a hypothetical role for some of the pertinent signalling pathways in phospho-regulation of cMyBP-C in the setting of heart failure.

KW - Animals

KW - Humans

KW - Binding Sites

KW - Substrate Specificity

KW - Phosphorylation

KW - Calcium/metabolism

KW - Signal Transduction

KW - Protein Kinase C/metabolism

KW - Calcium-Calmodulin-Dependent Protein Kinase Type 2/metabolism

KW - Carrier Proteins/metabolism

KW - Cyclic AMP-Dependent Protein Kinases/metabolism

KW - Heart Failure/metabolism/pathology

KW - Myofibrils/metabolism

KW - Ribosomal Protein S6 Kinases, 90-kDa/metabolism

KW - Animals

KW - Humans

KW - Binding Sites

KW - Substrate Specificity

KW - Phosphorylation

KW - Calcium/metabolism

KW - Signal Transduction

KW - Protein Kinase C/metabolism

KW - Calcium-Calmodulin-Dependent Protein Kinase Type 2/metabolism

KW - Carrier Proteins/metabolism

KW - Cyclic AMP-Dependent Protein Kinases/metabolism

KW - Heart Failure/metabolism/pathology

KW - Myofibrils/metabolism

KW - Ribosomal Protein S6 Kinases, 90-kDa/metabolism

M3 - SCORING: Journal article

VL - 33

SP - 53

EP - 60

JO - J MUSCLE RES CELL M

JF - J MUSCLE RES CELL M

SN - 0142-4319

IS - 1

M1 - 1

ER -