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, Jahrgang 33, Nr. 1, 1, 2012, S. 53-60.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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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 -