Association of the kinesin-binding domain of RanBP2 to KIF5B and KIF5C determines mitochondria localization and function.
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CLUH regulates mitochondrial biogenesis by binding mRNAs of nuclear-encoded mitochondrial proteinsRANBP2 is an allosteric activator of the conventional kinesin-1 motor protein, KIF5B, in a minimal cell-free systemHaploinsufficiency of RanBP2 is neuroprotective against light-elicited and age-dependent degeneration of photoreceptor neuronsTransporting mitochondria in neuronsAlterations in Mitochondrial Quality Control in Alzheimer's DiseaseAxonal transport: cargo-specific mechanisms of motility and regulationDynamics and diverse functions of nuclear pore complex proteinsThe axonal transport of mitochondriaMitochondrial transport in neurons: impact on synaptic homeostasis and neurodegeneration.Role of Ostm1 Cytosolic Complex with Kinesin 5B in Intracellular Dispersion and Trafficking.Bicaudal D2, dynein, and kinesin-1 associate with nuclear pore complexes and regulate centrosome and nuclear positioning during mitotic entryMolecular Basis for Specific Regulation of Neuronal Kinesin-3 Motors by Doublecortin Family ProteinsProtrudin serves as an adaptor molecule that connects KIF5 and its cargoes in vesicular transport during process formationMitochondrial trafficking in neuronsSunday Driver/JIP3 binds kinesin heavy chain directly and enhances its motility.Neuroprotection resulting from insufficiency of RANBP2 is associated with the modulation of protein and lipid homeostasis of functionally diverse but linked pathways in response to oxidative stress.KIF5B transports BNIP-2 to regulate p38 mitogen-activated protein kinase activation and myoblast differentiation.Chimeric Genes in Deletions and Duplications Associated with Intellectual DisabilityMitochondrial Aspects of Synaptic Dysfunction in Alzheimer's Disease.Loss of Ranbp2 in motoneurons causes disruption of nucleocytoplasmic and chemokine signaling, proteostasis of hnRNPH3 and Mmp28, and development of amyotrophic lateral sclerosis-like syndromesKinesin's light chains inhibit the head- and microtubule-binding activity of its tail.Selective impairment of a subset of Ran-GTP-binding domains of ran-binding protein 2 (Ranbp2) suffices to recapitulate the degeneration of the retinal pigment epithelium (RPE) triggered by Ranbp2 ablation.Targeted inactivation of kinesin-1 in pancreatic β-cells in vivo leads to insulin secretory deficiency.The cyclophilin-like domain of Ran-binding protein-2 modulates selectively the activity of the ubiquitin-proteasome system and protein biogenesis.Nesprins anchor kinesin-1 motors to the nucleus to drive nuclear distribution in muscle cells.Nucleoporin 62-like protein activates canonical Wnt signaling through facilitating the nuclear import of β-catenin in zebrafish.Analysis of Kif5b expression during mouse kidney development.Regulation of mitochondrial transport in neurons.Targeting the cyclophilin domain of Ran-binding protein 2 (Ranbp2) with novel small molecules to control the proteostasis of STAT3, hnRNPA2B1 and M-opsin.Disparate Regulatory Mechanisms Control Fat3 and P75NTR Protein Transport through a Conserved Kif5-Interaction DomainKinesin tail domains are intrinsically disordered.Ranbp2 haploinsufficiency mediates distinct cellular and biochemical phenotypes in brain and retinal dopaminergic and glia cells elicited by the Parkinsonian neurotoxin, 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP).Conventional kinesin holoenzymes are composed of heavy and light chain homodimers.Axonal transport and the delivery of pre-synaptic components.Mitochondrial trafficking and anchoring in neurons: New insight and implications.The meaning of mitochondrial movement to a neuron's lifeIntrinsic Disorder in the Kinesin Superfamily.Identification of Kinesin-1 Cargos Using Fluorescence Microscopy.Sumoylation in p27kip1 via RanBP2 promotes cancer cell growth in cholangiocarcinoma cell line QBC939.Infection-triggered familial or recurrent cases of acute necrotizing encephalopathy caused by mutations in a component of the nuclear pore, RANBP2.
P2860
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P2860
Association of the kinesin-binding domain of RanBP2 to KIF5B and KIF5C determines mitochondria localization and function.
description
2007 nî lūn-bûn
@nan
2007 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
Association of the kinesin-bin ...... ria localization and function.
@ast
Association of the kinesin-bin ...... ria localization and function.
@en
Association of the kinesin-bin ...... ria localization and function.
@nl
type
label
Association of the kinesin-bin ...... ria localization and function.
@ast
Association of the kinesin-bin ...... ria localization and function.
@en
Association of the kinesin-bin ...... ria localization and function.
@nl
prefLabel
Association of the kinesin-bin ...... ria localization and function.
@ast
Association of the kinesin-bin ...... ria localization and function.
@en
Association of the kinesin-bin ...... ria localization and function.
@nl
P2093
P2860
P1433
P1476
Association of the kinesin-bin ...... ria localization and function.
@en
P2093
Andrew Yeh
Azamat Aslanukov
Haiqing Yi
Kyoung-in Cho
Paulo A Ferreira
Yunfei Cai
P2860
P304
P356
10.1111/J.1600-0854.2007.00647.X
P577
2007-09-21T00:00:00Z