Monoubiquitination promotes calpain cleavage of the protein phosphatase 2A (PP2A) regulatory subunit α4, altering PP2A stability and microtubule-associated protein phosphorylation. - Wikidata - wikimedia - TriplyDB

Monoubiquitination promotes calpain cleavage of the protein phosphatase 2A (PP2A) regulatory subunit α4, altering PP2A stability and microtubule-associated protein phosphorylation.

Monoubiquitination promotes calpain cleavage of the protein phosphatase 2A (PP2A) regulatory subunit α4, altering PP2A stability and microtubule-associated protein phosphorylation.

http://www.wikidata.org/entity/Q30520621

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Protein phosphatase 2A dysfunction in Alzheimer's disease Solution structure of the microtubule-targeting COS domain of MID1 Visualization of subunit interactions and ternary complexes of protein phosphatase 2A in mammalian cells XLOS-observed mutations of MID1 Bbox1 domain cause domain unfolding.The ubiquitin E3 ligase NOSIP modulates protein phosphatase 2A activity in craniofacial development.MID1 catalyzes the ubiquitination of protein phosphatase 2A and mutations within its Bbox1 domain disrupt polyubiquitination of alpha4 but not of PP2Ac.TNF-related apoptosis-inducing ligand (TRAIL) regulates midline-1, thymic stromal lymphopoietin, inflammation, and remodeling in experimental eosinophilic esophagitis Novel p75 neurotrophin receptor ligand stabilizes neuronal calcium, preserves mitochondrial movement and protects against HIV associated neuropathogenesis Protein monoubiquitylation: targets and diverse functions 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.A computational framework for distinguishing direct versus indirect interactions in human functional protein-protein interaction networks.A Novel Human CAMK2A Mutation Disrupts Dendritic Morphology and Synaptic Transmission, and Causes ASD-Related Behaviors.The tyrosine phosphatase PTPN13/FAP-1 links calpain-2, TBI and tau tyrosine phosphorylation.Expression and regulation of type 2A protein phosphatases and alpha4 signalling in cardiac health and hypertrophy The E3 ubiquitin ligase midline 1 promotes allergen and rhinovirus-induced asthma by inhibiting protein phosphatase 2A activity.Proteomic View of the Crosstalk between Lactobacillus mucosae and Intestinal Epithelial Cells in Co-culture Revealed by Q Exactive-Based Quantitative Proteomics.Profiling the interactome of protein kinase C ζ by proteomics and bioinformatics.Structural and functional observations of the P151L MID1 mutation reveal alpha4 plays a significant role in X-linked Opitz Syndrome.

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P2860

Monoubiquitination promotes calpain cleavage of the protein phosphatase 2A (PP2A) regulatory subunit α4, altering PP2A stability and microtubule-associated protein phosphorylation.

http://www.wikidata.org/entity/Q30520621

description

2012 nî lūn-bûn

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2012 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի մայիսին հրատարակված գիտական հոդված

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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name

Monoubiquitination promotes ca ...... iated protein phosphorylation.

@ast

Monoubiquitination promotes ca ...... iated protein phosphorylation.

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type

label

Monoubiquitination promotes ca ...... iated protein phosphorylation.

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Monoubiquitination promotes ca ...... iated protein phosphorylation.

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Monoubiquitination promotes ca ...... iated protein phosphorylation.

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Monoubiquitination promotes ca ...... iated protein phosphorylation.

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P356

JBC.M112.368613

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Journal of Biological Chemistry

P1476

Monoubiquitination promotes ca ...... iated protein phosphorylation.

@en

P2093

Benjamin W Spiller

http://www.w3.org/2001/XMLSchema#string

Brian C Kraemer

http://www.w3.org/2001/XMLSchema#string

Brian E Wadzinski

http://www.w3.org/2001/XMLSchema#string

Chris R Guthrie

http://www.w3.org/2001/XMLSchema#string

Guy R Watkins

http://www.w3.org/2001/XMLSchema#string

Matthew D Mazalouskas

http://www.w3.org/2001/XMLSchema#string

Ning Wang

http://www.w3.org/2001/XMLSchema#string

Rey J Gomez

http://www.w3.org/2001/XMLSchema#string

Susann Schweiger

http://www.w3.org/2001/XMLSchema#string

P2860

The Opitz syndrome gene product, MID1, associates with microtubules

Two different classes of E2 ubiquitin-conjugating enzymes are required for the mono-ubiquitination of proteins and elongation by polyubiquitin chains with a specific topology

Opitz G/BBB syndrome, a defect of midline development, is due to mutations in a new RING finger gene on Xp22

Active transport of the ubiquitin ligase MID1 along the microtubules is regulated by protein phosphatase 2A

Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling

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.

The structure of Tap42/alpha4 reveals a tetratricopeptide repeat-like fold and provides insights into PP2A regulation

Structure of a Protein Phosphatase 2A Holoenzyme: Insights into B55-Mediated Tau Dephosphorylation

Alzheimer's disease: genes, proteins, and therapy

MID1, mutated in Opitz syndrome, encodes an ubiquitin ligase that targets phosphatase 2A for degradation

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24207-24215

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scholarly article

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10.1074/JBC.M112.368613

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29

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287

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22613722

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phosphorylation

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3397847

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