Title : The deacetylase SIRT1 promotes membrane localization and activation of Akt and PDK1 during tumorigenesis and cardiac hypertrophy.

Pub. Date : 2011 Jul 19

PMID : 21775285






7 Functional Relationships(s)
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1 Akt is activated during growth factor stimulation through a process that requires binding of Akt to phosphatidylinositol 3,4,5-trisphosphate (PIP(3)), which promotes membrane localization and phosphorylation of Akt by the upstream kinase PDK1 (phosphoinositide-dependent protein kinase 1). pip(3) thymoma viral proto-oncogene 1 Mus musculus
2 Akt is activated during growth factor stimulation through a process that requires binding of Akt to phosphatidylinositol 3,4,5-trisphosphate (PIP(3)), which promotes membrane localization and phosphorylation of Akt by the upstream kinase PDK1 (phosphoinositide-dependent protein kinase 1). pip(3) thymoma viral proto-oncogene 1 Mus musculus
3 Akt is activated during growth factor stimulation through a process that requires binding of Akt to phosphatidylinositol 3,4,5-trisphosphate (PIP(3)), which promotes membrane localization and phosphorylation of Akt by the upstream kinase PDK1 (phosphoinositide-dependent protein kinase 1). pip(3) thymoma viral proto-oncogene 1 Mus musculus
4 We show that Akt and PDK1 are acetylated at lysine residues in their pleckstrin homology domains, which mediate PIP(3) binding. pip(3) thymoma viral proto-oncogene 1 Mus musculus
5 Acetylation blocked binding of Akt and PDK1 to PIP(3), thereby preventing membrane localization and phosphorylation of Akt. pip(3) thymoma viral proto-oncogene 1 Mus musculus
6 Acetylation blocked binding of Akt and PDK1 to PIP(3), thereby preventing membrane localization and phosphorylation of Akt. pip(3) thymoma viral proto-oncogene 1 Mus musculus
7 Deacetylation by SIRT1 enhanced binding of Akt and PDK1 to PIP(3) and promoted their activation. pip(3) thymoma viral proto-oncogene 1 Mus musculus