Molecular determinants for PP2A substrate specificity: charged residues mediate dephosphorylation of tyrosine hydroxylase by the PP2A/B' regulatory subunit
about
Tyrosine hydroxylase and regulation of dopamine synthesisPP2A: more than a reset switch to activate pRB proteins during the cell cycle and in response to signaling cues.Global Phosphoproteomic Mapping of Early Mitotic Exit in Human Cells Identifies Novel Substrate Dephosphorylation MotifsStructure of the Ca2+-dependent PP2A heterotrimer and insights into Cdc6 dephosphorylationProtein kinase C-dependent dephosphorylation of tyrosine hydroxylase requires the B56δ heterotrimeric form of protein phosphatase 2AREDD1 enhances protein phosphatase 2A-mediated dephosphorylation of Akt to repress mTORC1 signaling.Determinants for Substrate Specificity of Protein Phosphatase 2A.Mutations in the PP2A regulatory subunit B family genes PPP2R5B, PPP2R5C and PPP2R5D cause human overgrowth.Whole genome expression profiling associates activation of unfolded protein response with impaired production and release of epinephrine after recurrent hypoglycemia.Selective proteasomal degradation of the B'β subunit of protein phosphatase 2A by the E3 ubiquitin ligase adaptor Kelch-like 15Lewy-like aggregation of α-synuclein reduces protein phosphatase 2A activity in vitro and in vivo.Protein phosphatase 2A is regulated by protein kinase Cα (PKCα)-dependent phosphorylation of its targeting subunit B56α at Ser41.Functions of B56-containing PP2As in major developmental and cancer signaling pathways.Complex molecular regulation of tyrosine hydroxylase.Carfilzomib induces leukaemia cell apoptosis via inhibiting ELK1/KIAA1524 (Elk-1/CIP2A) and activating PP2A not related to proteasome inhibition.PP2A as a master regulator of the cell cycle.Protein phosphatase 2A inhibition and subsequent cytoskeleton reorganization contributes to cell migration caused by microcystin-LR in human laryngeal epithelial cells (Hep-2).Mitotic exit: Determining the PP2A dephosphorylation programPhosphorylation Regulates Id2 Degradation and Mediates the Proliferation of Neural Precursor CellsProtein phosphatase 2A is involved in the tyrosine hydroxylase phosphorylation regulated by α-synuclein.Clk2 and B56β mediate insulin-regulated assembly of the PP2A phosphatase holoenzyme complex on Akt.Positive selection analysis highlights key positions in plant PP2A regulatory subunits.
P2860
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P2860
Molecular determinants for PP2A substrate specificity: charged residues mediate dephosphorylation of tyrosine hydroxylase by the PP2A/B' regulatory subunit
description
2010 nî lūn-bûn
@nan
2010 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Molecular determinants for PP2 ...... the PP2A/B' regulatory subunit
@ast
Molecular determinants for PP2 ...... the PP2A/B' regulatory subunit
@en
Molecular determinants for PP2 ...... the PP2A/B' regulatory subunit
@nl
type
label
Molecular determinants for PP2 ...... the PP2A/B' regulatory subunit
@ast
Molecular determinants for PP2 ...... the PP2A/B' regulatory subunit
@en
Molecular determinants for PP2 ...... the PP2A/B' regulatory subunit
@nl
prefLabel
Molecular determinants for PP2 ...... the PP2A/B' regulatory subunit
@ast
Molecular determinants for PP2 ...... the PP2A/B' regulatory subunit
@en
Molecular determinants for PP2 ...... the PP2A/B' regulatory subunit
@nl
P2860
P356
P1433
P1476
Molecular determinants for PP2 ...... the PP2A/B' regulatory subunit
@en
P2093
Amit Saraf
Elizabeth A Oberg
P2860
P304
P356
10.1021/BI902160T
P407
P577
2010-02-01T00:00:00Z