https://transhumanist.ru/index.php?action=history&feed=atom&title=PPP2R5C 2026-11-08T15:01:00Z История изменений этой страницы в вики MediaWiki 1.43.6 https://transhumanist.ru/index.php?title=PPP2R5C&diff=5277&oldid=prev 2021-05-12T13:37:07Z

<p>Новая страница: «Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform (PP2A B subunit isoform B&#039;-gamma) (PP2A B subunit isoform B56-gamma) (PP2A B subun...»</p> <p><b>Новая страница</b></p><div>Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform (PP2A B subunit isoform B&#039;-gamma) (PP2A B subunit isoform B56-gamma) (PP2A B subunit isoform PR61-gamma) (PP2A B subunit isoform R5-gamma) (Renal carcinoma antigen NY-REN-29) [KIAA0044]<br /> <br /> ==Publications==<br /> <br /> {{medline-entry<br /> |title=PP2A regulatory subunit PP2A-B&#039; counteracts S6K phosphorylation.<br /> |pubmed-url=https://pubmed.ncbi.nlm.nih.gov/20444422<br /> |abstract=The insulin/TOR signaling pathway plays a crucial role in animal homeostasis, sensing nutrient status to regulate organismal growth and metabolism. We identify here the Drosophila B&#039; regulatory subunit of PP2A (PP2A-B&#039;) as a novel, conserved component of the insulin pathway that specifically targets the PP2A holoenzyme to dephosphorylate S6K. PP2A-B&#039; knockout flies have elevated S6K phosphorylation and exhibit phenotypes typical of elevated insulin signaling such as reduced total body triglycerides and reduced longevity. We show that PP2A-B&#039; interacts with S6K both physically and genetically. The human homolog of PP2A-B&#039;, [[PPP2R5C]], also counteracts S6K1 phosphorylation, indicating a conserved mechanism in mammals. Since S6K affects development of cancer and metabolic disease, our data identify [[PPP2R5C]] as a novel factor of potential medical relevance.<br /> |mesh-terms=* Animals<br /> * Drosophila<br /> * Drosophila Proteins<br /> * Gene Knockout Techniques<br /> * Humans<br /> * Insulin<br /> * Longevity<br /> * Phosphoprotein Phosphatases<br /> * Phosphorylation<br /> * Protein Phosphatase 2<br /> * Ribosomal Protein S6 Kinases, 70-kDa<br /> * Signal Transduction<br /> * Triglycerides<br /> <br /> |full-text-url=https://sci-hub.do/10.1016/j.cmet.2010.03.015<br /> }}</div>

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