Phosphorylation and microtubule association of the Opitz syndrome protein mid-1 is regulated by protein phosphatase 2A via binding to the regulatory subunit alpha 4.
about
MID1 and MID2 homo- and heterodimerise to tether the rapamycin-sensitive PP2A regulatory subunit, alpha 4, to microtubules: implications for the clinical variability of X-linked Opitz GBBB syndrome and other developmental disordersCytokine activation of p38 mitogen-activated protein kinase and apoptosis is opposed by alpha-4 targeting of protein phosphatase 2A for site-specific dephosphorylation of MEK3.Active transport of the ubiquitin ligase MID1 along the microtubules is regulated by protein phosphatase 2AMig12, a novel Opitz syndrome gene product partner, is expressed in the embryonic ventral midline and co-operates with Mid1 to bundle and stabilize microtubulesThe biogenesis of active protein phosphatase 2A holoenzymes: a tightly regulated process creating phosphatase specificityX-linked Opitz syndrome: novel mutations in the MID1 gene and redefinition of the clinical spectrumInhibitor-2 regulates protein phosphatase-1 complexed with NimA-related kinase to induce centrosome separationNMR studies of the C-terminus of alpha4 reveal possible mechanism of its interaction with MID1 and protein phosphatase 2ADevelopmental expression of alpha4 protein phosphatase regulatory subunit in tissues affected by Opitz syndrome.The E3 ubiquitin ligase- and protein phosphatase 2A (PP2A)-binding domains of the Alpha4 protein are both required for Alpha4 to inhibit PP2A degradation.Alpha4 is a ubiquitin-binding protein that regulates protein serine/threonine phosphatase 2A ubiquitinationOverlapping binding sites in protein phosphatase 2A for association with regulatory A and alpha-4 (mTap42) subunits.Monoubiquitination promotes calpain cleavage of the protein phosphatase 2A (PP2A) regulatory subunit α4, altering PP2A stability and microtubule-associated protein phosphorylation.The phosphatase subunit tap42 functions independently of target of rapamycin to regulate cell division and survival in Drosophila.Control of mTORC1 signaling by the Opitz syndrome protein MID1.Tor signalling in bugs, brain and brawn.Microcystin-LR (MCLR) induces a compensation of PP2A activity mediated by α4 protein in HEK293 cells.MID1 catalyzes the ubiquitination of protein phosphatase 2A and mutations within its Bbox1 domain disrupt polyubiquitination of alpha4 but not of PP2Ac.Midline 1 controls polarization and migration of murine cytotoxic T cells.Identification and functional characterization of novel transcriptional enhancers involved in regulating human GLI3 expression during early development.Relationship between SPRY and B30.2 protein domains. Evolution of a component of immune defence?Mid1/Mid2 expression in craniofacial development and a literature review of X-linked opitz syndrome.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.X-linked microtubule-associated protein, Mid1, regulates axon development.PP2A as a master regulator of the cell cycle.Quantitative proteomics reveals novel protein interaction partners of PP2A catalytic subunit in pancreatic β-cellsProtein phosphatase 2A (PP2A)-specific ubiquitin ligase MID1 is a sequence-dependent regulator of translation efficiency controlling 3-phosphoinositide-dependent protein kinase-1 (PDPK-1).α4 is highly expressed in carcinogen-transformed human cells and primary human cancers.Protein phosphatase 2A plays an important role in migration of bone marrow stroma cells.Role of mTOR in the degradation of IRS-1: regulation of PP2A activity.Interaction analysis of the heterotrimer formed by the phosphatase 2A catalytic subunit, alpha4 and the mammalian ortholog of yeast Tip41 (TIPRL).Mechanism of midline defect-causing mutation P151L in MID1 revealed.Midline 1 directs lytic granule exocytosis and cytotoxicity of mouse killer T cells.A MID1 gene mutation in a patient with Opitz G/BBB syndrome that altered the 3D structure of SPRY domain.MID2 can substitute for MID1 and control exocytosis of lytic granules in cytotoxic T cells
P2860
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P2860
Phosphorylation and microtubule association of the Opitz syndrome protein mid-1 is regulated by protein phosphatase 2A via binding to the regulatory subunit alpha 4.
description
2001 nî lūn-bûn
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2001 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Phosphorylation and microtubul ...... the regulatory subunit alpha 4
@nl
Phosphorylation and microtubul ...... he regulatory subunit alpha 4.
@ast
Phosphorylation and microtubul ...... he regulatory subunit alpha 4.
@en
type
label
Phosphorylation and microtubul ...... the regulatory subunit alpha 4
@nl
Phosphorylation and microtubul ...... he regulatory subunit alpha 4.
@ast
Phosphorylation and microtubul ...... he regulatory subunit alpha 4.
@en
prefLabel
Phosphorylation and microtubul ...... the regulatory subunit alpha 4
@nl
Phosphorylation and microtubul ...... he regulatory subunit alpha 4.
@ast
Phosphorylation and microtubul ...... he regulatory subunit alpha 4.
@en
P2093
P2860
P356
P1476
Phosphorylation and microtubul ...... he regulatory subunit alpha 4.
@en
P2093
P2860
P304
P356
10.1073/PNAS.111154698
P407
P577
2001-05-22T00:00:00Z