Involvement of the p97-Ufd1-Npl4 complex in the regulated endoplasmic reticulum-associated degradation of inositol 1,4,5-trisphosphate receptors (Q28576636)

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English	Involvement of the p97-Ufd1-Npl4 complex in the regulated endoplasmic reticulum-associated degradation of inositol 1,4,5-trisphosphate receptors	scientific journal article

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scholarly article

1 reference

31 January 2017

Involvement of the p97-Ufd1-Npl4 complex in the regulated endoplasmic reticulum-associated degradation of inositol 1,4,5-trisphosphate receptors (English)

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31 January 2017

endoplasmic reticulum

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author name string

Kamil J. Alzayady

1

1 reference

31 January 2017

Margaret M. Panning

2

1 reference

31 January 2017

Grant G. Kelley

3

1 reference

31 January 2017

Richard J. H. Wojcikiewicz

4

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31 January 2017

language of work or name

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publication date

14 October 2005

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31 January 2017

Journal of Biological Chemistry

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31 January 2017

280

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31 January 2017

34530–34537

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31 January 2017

41

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31 January 2017

A membrane protein complex mediates retro-translocation from the ER lumen into the cytosol

1 reference

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A membrane protein required for dislocation of misfolded proteins from the ER

1 reference

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

1 reference

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Molecular perspectives on p97-VCP: progress in understanding its structure and diverse biological functions

1 reference

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17 March 2017

Inositol 1,4,5-trisphosphate receptor ubiquitination is mediated by mammalian Ubc7, a component of the endoplasmic reticulum-associated degradation pathway, and is inhibited by chelation of intracellular Zn2+

1 reference

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17 March 2017

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

1 reference

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Characterization of the mouse gene for the U-box-type ubiquitin ligase UFD2a

1 reference

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17 March 2017

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

1 reference

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

1 reference

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Functional ATPase activity of p97/valosin-containing protein (VCP) is required for the quality control of endoplasmic reticulum in neuronally differentiated mammalian PC12 cells

1 reference

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The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction

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AAA-ATPase p97/Cdc48p, a cytosolic chaperone required for endoplasmic reticulum-associated protein degradation

1 reference

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The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol

1 reference

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HRD4/NPL4 is required for the proteasomal processing of ubiquitinated ER proteins

1 reference

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U box proteins as a new family of ubiquitin-protein ligases

1 reference

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Endoplasmic reticulum (ER)-associated degradation of T cell receptor subunits. Involvement of ER-associated ubiquitin-conjugating enzymes (E2s)

1 reference

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A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly.

1 reference

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17 March 2017

p47 is a cofactor for p97-mediated membrane fusion

1 reference

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Muscarinic receptor activation down-regulates the type I inositol 1,4,5-trisphosphate receptor by accelerating its degradation

1 reference

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Role of the ubiquitin-proteasome pathway in regulating abundance of the cyclin-dependent kinase inhibitor p27

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p97 and close encounters of every kind: a brief review

1 reference

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Bortezomib rapidly suppresses ubiquitin thiolesterification to ubiquitin-conjugating enzymes and inhibits ubiquitination of histones and type I inositol 1,4,5-trisphosphate receptor

1 reference

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Inositol 1,4,5-trisphosphate receptors as signal integrators

1 reference

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Subcellular distribution of the inositol 1,4,5-trisphosphate receptors: functional relevance and molecular determinants

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IP(3) receptors: the search for structure.

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Ubiquitylation as a quality control system for intracellular proteins.

1 reference

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For whom the bell tolls: protein quality control of the endoplasmic reticulum and the ubiquitin-proteasome connection

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ER-associated degradation in protein quality control and cellular regulation

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Ligand binding directly stimulates ubiquitination of the inositol 1, 4,5-trisphosphate receptor

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Expression of inositol trisphosphate receptors.

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Inositol 1,4,5-trisphosphate receptor down-regulation is activated directly by inositol 1,4,5-trisphosphate binding. Studies with binding-defective mutant receptors

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

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p97, a protein coping with multiple identities

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In vivo ubiquitination and proteasome-mediated degradation of p53(1)

1 reference

https://pubmed.ncbi.nlm.nih.gov/16103111

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Down-regulation of the inositol 1,4,5-trisphosphate receptor in mouse eggs following fertilization or parthenogenetic activation

1 reference

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Endoplasmic reticulum-associated protein degradation

1 reference

https://pubmed.ncbi.nlm.nih.gov/16103111

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based on heuristic

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Identifiers

10.1074/JBC.M508890200

1 reference

31 January 2017

release_jhvelbz6ivevdksw55vytqfwkm

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24 November 2022

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mapped directly with Wikidata item

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1 reference

31 January 2017

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