The calcium transport mechanism of cardiac sarcoplasmic reticulum (SR) is (SR) is regulated by a phosphoregulatory mechanism involving the phosphorylation-dephosphorylation of an integral membrane component, termed phospholamban. Phospholamban, a 27,000 Da proteolipid, contains phosphorylation sites
The role of protein kinases and protein phosphatases in the regulation of cardiac sarcoplasmic reticulum function
โ Scribed by Evangelia G. Kranias; Ramesh C. Gupta; Gyorgyi Jakab; Hae Won Kim; Nancy A. E. Steenaart; Stephen T. Rapundalo
- Publisher
- Springer
- Year
- 1988
- Tongue
- English
- Weight
- 585 KB
- Volume
- 82
- Category
- Article
- ISSN
- 0300-8177
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โฆ Synopsis
Canine cardiac sarcoplasmic reticulum is phosphorylated by adenosine 3',5'-monophosphate (cAMP)-dependent and by calcium.calmodulin-dependent protein kinases on a 27,000 proteolipid, called phospholamban. Both types of phosphorylation are associated with an increase in the initial rates of Ca2+ transport by SR vesicles which reflects an increased turnover of elementary steps of the calcium ATPase reaction sequence. The stimulatory effects of the protein kinases on the calcium pump may be reversed by an endogenous protein phosphatase, which can dephosphorylate both the cAMP-dependent and the calcium.calmodulin-dependent sites on phospholamban. Thus, the calcium pump in cardiac sarcoplasmic reticulum appears to be under reversible regulation mediated by protein kinases and protein phosphatases.
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Intracellular signaling proteins are very often regulated by site-specific phosphorylation. For example, growth factor receptors in eukaryotic cells contain intrinsic tyrosine kinase activity and use inter- and intra-molecular interactions to recruit and orient potential protein substrates for phosp