Variations on a theme: Transcriptional regulation mediated through post-translational modification and microRNA function.

Overview

Cytosolic PLA2 (cPLA2alpha) is a member of a large family of lipolytic enzymes that catalyze the hydrolysis of the fatty acid ester at the sn-2 position of the phospholipids. cPLA2alpha selectively liberates arachidonic acid from membrane phospholipids. Cellular cPLA2alpha activities are tightly regulated by different factors, including Ca2+, phosphorylation, lipid mediators, and other cellular proteins. The catalytic domain of cPLA2alpha contains several phosphorylation sites, Ser454, Ser437, Ser505, Ser515, and...
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Overview

Cytosolic PLA2 (cPLA2alpha) is a member of a large family of lipolytic enzymes that catalyze the hydrolysis of the fatty acid ester at the sn-2 position of the phospholipids. cPLA2alpha selectively liberates arachidonic acid from membrane phospholipids. Cellular cPLA2alpha activities are tightly regulated by different factors, including Ca2+, phosphorylation, lipid mediators, and other cellular proteins. The catalytic domain of cPLA2alpha contains several phosphorylation sites, Ser454, Ser437, Ser505, Ser515, and Ser727. Phosphorylation of different serines of cPLA2alpha has been shown to activate cPLA2alpha; however, the physiological significance of multi-site phosphorylation of cPLA2alpha and the mechanism by which the phosphorylation activates cPLA2alpha have not been fully elucidated. In our study, we demonstrated that phosphorylation of Ser727 regulates the cellular cPLA2alpha activity by modulating its interaction with p11 on the basis of the report that p11 interacts with the C-terminal region of cPLA2alpha where Ser727 is located. Extensive in vitro and cellular membrane binding and activity measurements using cPLA2alpha wild type and mutants provided evidence that phosphorylation of Ser727 regulates the cellular cPLA 2alpha activity by modulating its interaction with A2t, but not p11 alone, which binds to the hydroxyl group of Ser727 and thereby interferes with its membrane binding. To investigate the mechanism underlying the cPLA2alpha activation by multi-site phosphorylation and systematically study the regulation by five different phosphorylation sites individually, all the candidate phosphorylation sites were mutated. A whole set of phosphorylation and de-phosphorylation mimicking mutants were constructed. It was shown that at low Ca2+ concentration, phosphorylation of Ser505 had the largest effect on the activation of cPLA2alpha by slowing down the membrane dissociation of the enzyme; while at high Ca2+ concentration, phosphorylation of other serines activated the enzyme as well as that of Ser 505. Our studies for the first time systematically investigate how multiple sites phosphorylation activates cPLA2alpha identify the level of [Ca2+]i when only one phosphorylation play the major regulatory function. Our dates also suggest the possible role of [Ca2+]i in effecting the activation of cPLA 2alpha by different phosphorylations.
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Product Details

  • ISBN-13: 9781243545329
  • Publisher: BiblioLabsII
  • Publication date: 9/3/2011
  • Pages: 142
  • Product dimensions: 7.44 (w) x 9.69 (h) x 0.30 (d)

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