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Protein Phosphatase-1 Dephosphorylates Akt1 at Thr-450 to Modulates Its Functions

Author: YuanDan
Tutor: LiWanCheng；FengHao
School: Hunan Normal University
Course: Cell Biology
Keywords: Protein kinase B Protein phosphatase -1 Dephosphorylated Signal Transduction
CLC: Q55
Type: Master's thesis
Year: 2009
Downloads: 27
Quote: 0
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Abstract


Protein kinase B ( PKB / AKT ) signaling pathways in cell proliferation , cell differentiation, cell survival signal transduction regulatory process plays a key role . Previous studies have shown PKB / AKT activation is done through a series of phosphorylation process : First , prior to the activation of PKB / AKT Thr450 sites of c-Jun amino -terminal kinase ( JNK ) phosphorylation . Then phosphoinositide -dependent protein kinase -1 ( PDK1 ) phosphorylation of AKT THR - 308 sites , Ser - 473 residues exposed . Finally, some kinase ( the PKD2 and other kinase ) phosphorylation of AKT Ser473 sites makes PKB / Akt is fully activated . PH domain - containing phosphatase AKT Ser473 sites or Thr308 point dephosphorylated , and can lead to the inactivation of PKB / Akt . In addition , protein phosphatase - 2A ( PP - 2A ) also works Thr308 AKT sites dephosphorylated . However dephosphorylation of the Thr450 sites which led to the complete inactivation of AKT phosphatase unclear . In our study , by in vivo and in vitro experiments show that the the AKT1 protein phosphatase -1 ( PP - 1 ) dephosphorylation of the key so that it completely inactivated protein phosphatase . First , the PP-1 in vitro AKT direct dephosphorylation reaction . Immune co-precipitation Western blot analysis showed that the interaction of PP -1 and AKT . Again , calyculin A inhibition or specific siRNA silencing PP - 1 , AKT1 Thr450 sites can hyperphosphorylation . Finally, in the human lens epithelial cells and retinal pigment epithelial cells , overexpression of PP - 1 and PP-2A , AKT1 Thr450 phosphorylation sites significantly reduced . These results are integrated together, confirmed in human lens epithelial cells and retinal pigment epithelial cells , PP - 1 , thereby regulating the function of the protein phosphatase dephosphorylation AKT1 Thr450 sites .

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