Parkin-mediated monoubiquitination of the PDZ protein PICK1 regulates the activity of acid-sensing ion channels - Test2 - elhamkhani - TriplyDB

Parkin-mediated monoubiquitination of the PDZ protein PICK1 regulates the activity of acid-sensing ion channels

Parkin-mediated monoubiquitination of the PDZ protein PICK1 regulates the activity of acid-sensing ion channels

http://www.wikidata.org/entity/Q24679424

about

UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids Autoregulation of Parkin activity through its ubiquitin-like domain Parkin-dependent degradation of the F-box protein Fbw7β promotes neuronal survival in response to oxidative stress by stabilizing Mcl-1 Ubiquitin-proteasome system as a modulator of cell fate Novel Insights into Acid-Sensing Ion Channels: Implications for Degenerative Diseases Emerging preclinical pharmacological targets for Parkinson's disease Proteostasis and RNA Binding Proteins in Synaptic Plasticity and in the Pathogenesis of Neuropsychiatric Disorders Parkin Regulation and Neurodegenerative Disorders Ubiquitin-dependent trafficking and turnover of ionotropic glutamate receptors RBR E3 ubiquitin ligases: new structures, new insights, new questions Acid-sensing ion channels in pain and disease.Syntabulin regulates the trafficking of PICK1-containing vesicles in neurons.Parkin and PINK1 function in a vesicular trafficking pathway regulating mitochondrial quality control The parkin-like human homolog of Drosophila ariadne-1 (HHARI) can induce aggresome formation in mammalian cells and is immunologically detectable in Lewy bodies Aggresome formation and neurodegenerative diseases: therapeutic implications Parkin deficiency delays motor decline and disease manifestation in a mouse model of synucleinopathy Pruning and loss of excitatory synapses by the parkin ubiquitin ligase Parkin promotes degradation of the mitochondrial pro-apoptotic ARTS protein Drosophila parkin requires PINK1 for mitochondrial translocation and ubiquitinates mitofusin The PINK1/Parkin pathway regulates mitochondrial morphology The PINK1/Parkin pathway regulates mitochondrial dynamics and function in mammalian hippocampal and dopaminergic neurons.Parkin-mediated ubiquitination regulates phospholipase C-gamma1.Small, N-terminal tags activate Parkin E3 ubiquitin ligase activity by disrupting its autoinhibited conformation.Parkin regulates kainate receptors by interacting with the GluK2 subunit An essential postsynaptic role for the ubiquitin proteasome system in slow homeostatic synaptic plasticity in cultured hippocampal neurons.Upregulation of Parkin in endophilin mutant mice.Loss of Acid sensing ion channel-1a and bicarbonate administration attenuate the severity of traumatic brain injury Altered hippocampal synaptic physiology in aged parkin-deficient mice.Ubiquitination in postsynaptic function and plasticity The E3 ubiquitin ligase parkin is recruited to the 26 S proteasome via the proteasomal ubiquitin receptor Rpn13 Parkin mediates the degradation-independent ubiquitination of Hsp70 Ataxin-3 deubiquitination is coupled to Parkin ubiquitination via E2 ubiquitin-conjugating enzyme.Acid-sensing ion channels: potential therapeutic targets for neurologic diseases.ENaCs and ASICs as therapeutic targets.Protein monoubiquitylation: targets and diverse functions Ubiquitination of neurotransmitter receptors and postsynaptic scaffolding proteins Parkin deficiency contributes to pancreatic tumorigenesis by inducing spindle multipolarity and misorientation.Covalent ISG15 conjugation positively regulates the ubiquitin E3 ligase activity of parkin AF-6 is a positive modulator of the PINK1/parkin pathway and is deficient in Parkinson's disease.The role of PTEN-induced kinase 1 in mitochondrial dysfunction and dynamics.

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P2860

Parkin-mediated monoubiquitination of the PDZ protein PICK1 regulates the activity of acid-sensing ion channels

http://www.wikidata.org/entity/Q24679424

description

2007 nî lūn-bûn

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2007 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

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2007 թվականի օգոստոսին հրատարակված գիտական հոդված

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2007年の論文

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2007年論文

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Parkin-mediated monoubiquitina ...... y of acid-sensing ion channels

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Parkin-mediated monoubiquitina ...... y of acid-sensing ion channels

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Parkin-mediated monoubiquitina ...... y of acid-sensing ion channels

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Parkin-mediated monoubiquitina ...... y of acid-sensing ion channels

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Parkin-mediated monoubiquitina ...... y of acid-sensing ion channels

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Parkin-mediated monoubiquitina ...... y of acid-sensing ion channels

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Parkin-mediated monoubiquitina ...... y of acid-sensing ion channels

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Parkin-mediated monoubiquitina ...... y of acid-sensing ion channels

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MBC.E05-11-1027

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Molecular Biology of the Cell

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Parkin-mediated monoubiquitina ...... y of acid-sensing ion channels

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Amadou T Corera

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Ariel R Ase

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Carol X-Q Chen

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Maria Kontogiannea

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Monica Joch

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Penny A MacDonald

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Philippe Séguéla

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P2860

RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent ubiquitination

Familial Parkinson disease gene product, parkin, is a ubiquitin-protein ligase

Parkin functions as an E2-dependent ubiquitin- protein ligase and promotes the degradation of the synaptic vesicle-associated protein, CDCrel-1

Functional interaction between monoamine plasma membrane transporters and the synaptic PDZ domain-containing protein PICK1

An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin

Parkin ubiquitinates the alpha-synuclein-interacting protein, synphilin-1: implications for Lewy-body formation in Parkinson disease

Interaction of the synaptic protein PICK1 (protein interacting with C kinase 1) with the non-voltage gated sodium channels BNC1 (brain Na+ channel 1) and ASIC (acid-sensing ion channel)

Parkin mediates nonclassical, proteasomal-independent ubiquitination of synphilin-1: implications for Lewy body formation

The acid-activated ion channel ASIC contributes to synaptic plasticity, learning, and memory

Parkin is a component of an SCF-like ubiquitin ligase complex and protects postmitotic neurons from kainate excitotoxicity

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3105-18

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scholarly article

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4370889

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10.1091/MBC.E05-11-1027

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8

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