期刊
JOURNAL OF MUSCLE RESEARCH AND CELL MOTILITY
卷 33, 期 1, 页码 53-60出版社
SPRINGER
DOI: 10.1007/s10974-011-9276-3
关键词
cMyBP-C; Phosphorylation; Protein kinases; Adrenergic receptors; Heart failure; Protein kinase D; p90 ribosomal S6 kinase
类别
资金
- British Heart Foundation [PG/03/053, FS/03/091, PG/05/043, PG/07/056/23150, PG/08/064/25398]
- Medical Research Council [G0001112, G0001227, G0300052, G0800206]
- British Heart Foundation [PG/11/9/28705, PG/11/100/29211] Funding Source: researchfish
- Medical Research Council [G0300052, G0001112, G0800206] Funding Source: researchfish
- MRC [G0001112, G0300052, G0800206] Funding Source: UKRI
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 Ca2+/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.
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