The E3 ubiquitin ligase- and protein phosphatase 2A (PP2A)-binding domains of the Alpha4 protein are both required for Alpha4 to inhibit PP2A degradation.
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The biogenesis of active protein phosphatase 2A holoenzymes: a tightly regulated process creating phosphatase specificityStructural basis of protein phosphatase 2A stable latencyNMR studies of the C-terminus of alpha4 reveal possible mechanism of its interaction with MID1 and protein phosphatase 2AProtein Phosphatase Methyl-Esterase PME-1 Protects Protein Phosphatase 2A from Ubiquitin/Proteasome DegradationXLOS-observed mutations of MID1 Bbox1 domain cause domain unfolding.Monoubiquitination promotes calpain cleavage of the protein phosphatase 2A (PP2A) regulatory subunit α4, altering PP2A stability and microtubule-associated protein phosphorylation.Interaction between salt-inducible kinase 2 and protein phosphatase 2A regulates the activity of calcium/calmodulin-dependent protein kinase I and protein phosphatase methylesterase-1.Essential roles of the Tap42-regulated protein phosphatase 2A (PP2A) family in wing imaginal disc development of Drosophila melanogaster.MID1 catalyzes the ubiquitination of protein phosphatase 2A and mutations within its Bbox1 domain disrupt polyubiquitination of alpha4 but not of PP2Ac.A gatekeeper chaperone complex directs translocator secretion during type three secretion.Molecular dynamics simulation reveals insights into the mechanism of unfolding by the A130T/V mutations within the MID1 zinc-binding Bbox1 domain.Mid1/Mid2 expression in craniofacial development and a literature review of X-linked opitz syndrome.Crystal structure of the human Tip41 orthologue, TIPRL, reveals a novel fold and a binding site for the PP2Ac C-terminus.The MID1 E3 ligase catalyzes the polyubiquitination of Alpha4 (α4), a regulatory subunit of protein phosphatase 2A (PP2A): novel insights into MID1-mediated regulation of PP2A.All roads lead to PP2A: exploiting the therapeutic potential of this phosphatase.Quantitative proteomics reveals novel protein interaction partners of PP2A catalytic subunit in pancreatic β-cellsTargeted deep resequencing identifies MID2 mutation for X-linked intellectual disability with varied disease severity in a large kindred from India.Identification and characterization of an alternatively spliced isoform of the human protein phosphatase 2Aα catalytic subunitExpression and regulation of type 2A protein phosphatases and alpha4 signalling in cardiac health and hypertrophyA receptor-interacting protein 1 (RIP1)-independent necrotic death under the control of protein phosphatase PP2A that involves the reorganization of actin cytoskeleton and the action of cofilin-1.Discovery of new substrates of the elongation factor-2 kinase suggests a broader role in the cellular nutrient response.Structural and functional observations of the P151L MID1 mutation reveal alpha4 plays a significant role in X-linked Opitz Syndrome.Effects of cerulein on keratin 8 phosphorylation and perinuclear reorganization in pancreatic cancer cells: Involvement of downregulation of protein phosphatase 2A and alpha4.
P2860
Q26824764-30A8921B-6416-4329-B64B-63F5B1E41239Q27677410-5E61F74E-82BE-47BD-9FC2-F7ABA8F63999Q28478425-F5E387CE-92D9-437A-ADF3-A9A1319DB463Q28551570-8E0B85C1-1F23-439F-AC5E-EC20B10164D3Q30366739-53C3565A-4618-45A0-B8EE-A72324237B33Q30520621-D7BDA4EF-4737-417F-84B2-5500482FAB08Q33947256-4DB23DD8-6F28-47BB-B6DE-D75F0F8C1048Q34305548-0674CDEF-E533-4641-8AE3-552280E3ABA9Q35245786-A7C289DA-8193-4763-97F3-97DAA4F5ED91Q35398859-3E4524DE-30F6-4277-A11E-DE9057018C99Q35601459-B0A3BAFF-0072-4FA1-B245-F9523FE1755EQ36447391-5E3BF098-2593-4695-966B-57F04060F95EQ37151237-2D56CFD7-2042-49D6-B7FD-2ACF437BF931Q37175200-C9690CBB-9C8E-41CA-921F-A6800322A066Q38617799-021DCADE-0CA3-438F-9A80-849C8B6F49B2Q38794957-4F9B071C-CADB-411F-8071-9B6E6EC4F650Q39081888-DCB07B7F-DE98-4A6B-BF9E-2BD945519712Q41225103-02A2FF55-B1F3-4B39-AEA2-2CA320DACD49Q41842719-523B26D5-6ABF-4E66-80B4-7FFEA62DF649Q41947183-2B9A2136-D463-4E34-BC65-B9E4D5E08F04Q47142189-636BA5B9-77BA-458D-BC30-46E099C8DBB1Q50977728-678DA347-1691-4A55-B8E2-A9606968C179Q53199897-443CBA43-A54A-4238-9352-6E3FE7D1B2EF
P2860
The E3 ubiquitin ligase- and protein phosphatase 2A (PP2A)-binding domains of the Alpha4 protein are both required for Alpha4 to inhibit PP2A degradation.
description
2011 nî lūn-bûn
@nan
2011 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի մարտին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
The E3 ubiquitin ligase- and p ...... 4 to inhibit PP2A degradation.
@ast
The E3 ubiquitin ligase- and p ...... 4 to inhibit PP2A degradation.
@en
type
label
The E3 ubiquitin ligase- and p ...... 4 to inhibit PP2A degradation.
@ast
The E3 ubiquitin ligase- and p ...... 4 to inhibit PP2A degradation.
@en
prefLabel
The E3 ubiquitin ligase- and p ...... 4 to inhibit PP2A degradation.
@ast
The E3 ubiquitin ligase- and p ...... 4 to inhibit PP2A degradation.
@en
P2093
P2860
P356
P1476
The E3 ubiquitin ligase- and p ...... 4 to inhibit PP2A degradation.
@en
P2093
Benjamin W Spiller
Brian E Wadzinski
Guy R Watkins
Katherine L Germane
Lisa R McCorvey
Michele LeNoue-Newton
P2860
P304
17665-17671
P356
10.1074/JBC.M111.222414
P407
P577
2011-03-29T00:00:00Z