The AAA ATPase p97/VCP interacts with its alternative co-factors, Ufd1-Npl4 and p47, through a common bipartite binding mechanism. - Wikidata - awgldk - TriplyDB

The AAA ATPase p97/VCP interacts with its alternative co-factors, Ufd1-Npl4 and p47, through a common bipartite binding mechanism.

The AAA ATPase p97/VCP interacts with its alternative co-factors, Ufd1-Npl4 and p47, through a common bipartite binding mechanism.

http://www.wikidata.org/entity/Q45061748

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Multilayered mechanism of CD4 downregulation by HIV-1 Vpu involving distinct ER retention and ERAD targeting steps Identification of VCP/p97, carboxyl terminus of Hsp70-interacting protein (CHIP), and amphiphysin II interaction partners using membrane-based human proteome arrays UBXD7 binds multiple ubiquitin ligases and implicates p97 in HIF1alpha turnover The UBX protein SAKS1 negatively regulates endoplasmic reticulum-associated degradation and p97-dependent degradation Detailed structural insights into the p97-Npl4-Ufd1 interface The Structural and Functional Basis of the p97/Valosin-containing Protein (VCP)-interacting Motif (VIM): MUTUALLY EXCLUSIVE BINDING OF COFACTORS TO THE N-TERMINAL DOMAIN OF p97 Structural Basis for Ovarian Tumor Domain-containing Protein 1 (OTU1) Binding to p97/Valosin-containing Protein (VCP)The budding yeast Cdc48(Shp1) complex promotes cell cycle progression by positive regulation of protein phosphatase 1 (Glc7).The ER-associated degradation component Der1p and its homolog Dfm1p are contained in complexes with distinct cofactors of the ATPase Cdc48p Sel1p/Ubx2p participates in a distinct Cdc48p-dependent endoplasmic reticulum-associated degradation pathway.Ubx4 modulates cdc48 activity and influences degradation of misfolded proteins of the endoplasmic reticulum A conserved protein with AN1 zinc finger and ubiquitin-like domains modulates Cdc48 (p97) function in the ubiquitin-proteasome pathway The p97 ATPase associates with EEA1 to regulate the size of early endosomes The general definition of the p97/valosin-containing protein (VCP)-interacting motif (VIM) delineates a new family of p97 cofactors Hereditary inclusion body myopathy-linked p97/VCP mutations in the NH2 domain and the D1 ring modulate p97/VCP ATPase activity and D2 ring conformation Control of p97 function by cofactor binding Conformational changes in the AAA ATPase p97-p47 adaptor complex Protection of armadillo/β-Catenin by armless, a novel positive regulator of wingless signaling Structural Details of Ufd1 Binding to p97 and Their Functional Implications in ER-Associated Degradation Wss1 metalloprotease partners with Cdc48/Doa1 in processing genotoxic SUMO conjugates Involvement of the p97-Ufd1-Npl4 complex in the regulated endoplasmic reticulum-associated degradation of inositol 1,4,5-trisphosphate receptors Small but versatile: the extraordinary functional and structural diversity of the beta-grasp fold A Mighty "Protein Extractor" of the Cell: Structure and Function of the p97/CDC48 ATPase.Regulation of mitochondrial genome inheritance by autophagy and ubiquitin-proteasome system: implications for health, fitness, and fertility Delivery of ubiquitinated substrates to protein-unfolding machines.The p97 ATPase dislocates MHC class I heavy chain in US2-expressing cells via a Ufd1-Npl4-independent mechanism.Derlin-1 regulates mutant VCP-linked pathogenesis and endoplasmic reticulum stress-induced apoptosis.Functional chromatography reveals three natural products that target the same protein with distinct mechanisms of action.p97-containing complexes in proliferation control and cancer: emerging culprits or guilt by association?ATP binding to p97/VCP D1 domain regulates selective recruitment of adaptors to its proximal N-domain.The complexities of p97 function in health and disease Ubiquitin-recognition protein Ufd1 couples the endoplasmic reticulum (ER) stress response to cell cycle control.Concerted action of the ubiquitin-fusion degradation protein 1 (Ufd1) and Sumo-targeted ubiquitin ligases (STUbLs) in the DNA-damage response.Derlin-1 is a rhomboid pseudoprotease required for the dislocation of mutant α-1 antitrypsin from the endoplasmic reticulum.Structural insights into the p97-Ufd1-Npl4 complex.Distinct conformations of the protein complex p97-Ufd1-Npl4 revealed by electron cryomicroscopy Chromatin-associated degradation is defined by UBXN-3/FAF1 to safeguard DNA replication fork progression.Complex of Fas-associated factor 1 (FAF1) with valosin-containing protein (VCP)-Npl4-Ufd1 and polyubiquitinated proteins promotes endoplasmic reticulum-associated degradation (ERAD)Structural and functional deviations in disease-associated p97 mutants.VCP and ATL1 regulate endoplasmic reticulum and protein synthesis for dendritic spine formation

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P2860

The AAA ATPase p97/VCP interacts with its alternative co-factors, Ufd1-Npl4 and p47, through a common bipartite binding mechanism.

http://www.wikidata.org/entity/Q45061748

description

2004 nî lūn-bûn

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2004年の論文

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2004年学术文章

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2004年学术文章

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2004年学术文章

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2004年学术文章

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2004年学术文章

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2004年学术文章

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2004年學術文章

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2004年學術文章

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name

The AAA ATPase p97/VCP interac ...... n bipartite binding mechanism.

@en

The AAA ATPase p97/VCP interac ...... n bipartite binding mechanism.

@nl

type

label

The AAA ATPase p97/VCP interac ...... n bipartite binding mechanism.

@en

The AAA ATPase p97/VCP interac ...... n bipartite binding mechanism.

@nl

prefLabel

The AAA ATPase p97/VCP interac ...... n bipartite binding mechanism.

@en

The AAA ATPase p97/VCP interac ...... n bipartite binding mechanism.

@nl

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P2860

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P1433

Journal of Biological Chemistry

P1476

The AAA ATPase p97/VCP interac ...... n bipartite binding mechanism.

@en

P2093

Catherine Brasseur

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

Hemmo H Meyer

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

Roland M Bruderer

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

P2860

CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice

Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains

Direct binding of ubiquitin conjugates by the mammalian p97 adaptor complexes, p47 and Ufd1-Npl4.

A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways

VCIP135, a novel essential factor for p97/p47-mediated membrane fusion, is required for Golgi and ER assembly in vivo

VCIP135 acts as a deubiquitinating enzyme during p97-p47-mediated reassembly of mitotic Golgi fragments

The solution structure of VAT-N reveals a 'missing link' in the evolution of complex enzymes from a simple betaalphabetabeta element

Structure of the AAA ATPase p97

The UBX domain: a widespread ubiquitin-like module

Solution structure and interaction surface of the C-terminal domain from p47: a major p97-cofactor involved in SNARE disassembly

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49609-49616

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scholarly article

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10.1074/JBC.M408695200

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48

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279

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2004-09-15T00:00:00Z

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15371428

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