Involvement of the p97-Ufd1-Npl4 Complex in the Regulated Endoplasmic Reticulum-associated Degradation of Inositol 1,4,5-Trisphosphate Receptors

Alzayady, Kamil J.; Panning, Margaret M.; Kelley, Grant G.; Richard Wojcikiewicz, J.H.

doi:10.1074/jbc.m508890200

Cited by 47Ubiquitin and proteasome pathwaysEndoplasmic Reticulum Stress and DiseaseHeat shock proteins research

Involvement of the p97-Ufd1-Npl4 Complex in the Regulated Endoplasmic Reticulum-associated Degradation of Inositol 1,4,5-Trisphosphate Receptors

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Alzayady, Kamil J., Panning, Margaret M., Kelley, Grant G., Richard Wojcikiewicz, J.H.·2005·Journal of Biological Chemistry

DOI 10.1074/jbc.m508890200PMC PMC1483127

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Abstract

Inositol 1,4,5-trisphosphate (IP(3)) receptors form tetrameric, IP(3)-gated channels in endoplasmic reticulum membranes that govern the release of Ca(2+) from this organelle. In response to activation of certain G protein-coupled receptors that persistently elevate IP(3) concentration, IP(3) receptors are ubiquitinated and degraded by the ubiquitin-proteasome pathway. IP(3) receptor ubiquitination is mediated by the ubiquitin-conjugating enzyme, (mam)Ubc7, a component of the endoplasmic reticulum-associated degradation pathway. However, the mechanism by which ubiquitinated IP(3) receptors are transferred to the proteasome is not known. Here, we examine this process and show in several mammalian cell types that the ATPase p97 associates with IP(3) receptors in response to hormonal stimuli that induce IP(3) receptor ubiquitination. To examine the functional relevance of the p97 interaction with IP(3) receptors, we stably and specifically reduced p97 protein levels by 62 +/- 3% in Rat-1 fibroblasts using RNA interference. In these cells, endothelin-1-induced IP(3) receptor degradation was markedly retarded and the accumulation of ubiquitinated IP(3) receptors was markedly enhanced. These effects were reversed by expression of exogenous p97. In addition, Ufd1 and Npl4, which complex with p97, also associated with IP(3) receptors upon hormonal stimulation. We conclude that the p97-Ufd1-Npl4 complex couples ubiquitinated IP(3) receptors to proteasomal degradation and, thus, plays a…

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The p97-Ufd1-Npl4 complex participates in the delivery of polyubiquitinated IP3 receptors to the proteasome.
“This p97-Ufd1-Npl4 complex participates in the delivery of polyubiquitinated IP 3 receptors to the proteasome (4).”
From RNF170 Protein, an Endoplasmic Reticulum Membrane Ubiquitin Ligase, Mediates Inositol 1,4,5-Trisphosphate Receptor Ubiquitination and Degradation (2011) · cites this paper as [4]
IP3 receptor down-regulation has been demonstrated in many mammalian cell types, including GnRH-stimulated αT3-1 mouse pituitary gonadotropes, ET1-stimulated Rat1 fibroblasts, muscarinic agonist-stimulated SH-SY5Y human neuroblastoma cells, and mHeLa cells.
“This IP 3 receptor 'down-regulation' has been demonstrated in many mammalian cell types, including gonadotropin-releasing hormone (GnRH)-stimulated 𝛂 T3-1 mouse pituitary gonadotropes (3), endothelin 1 (ET1)-stimulated Rat1 fibroblasts (4), and muscarinic agonist-stimulated SH-SY5Y human neuroblastoma cells (5) and mHeLa cells (6).”
From RNF170 Protein, an Endoplasmic Reticulum Membrane Ubiquitin Ligase, Mediates Inositol 1,4,5-Trisphosphate Receptor Ubiquitination and Degradation (2011) · cites this paper as [4]
p97 associates with IP3 receptors after they have been polyubiquitinated.
“which associates with IP 3 receptors after they have been polyubiquitinated (4, 14, 15).”
From RNF170 Protein, an Endoplasmic Reticulum Membrane Ubiquitin Ligase, Mediates Inositol 1,4,5-Trisphosphate Receptor Ubiquitination and Degradation (2011) · cites this paper as [4]

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Self-citation

Authors: Alzayady, K. J., Panning, M. M., Kelley, G. G., & Richard Wojcikiewicz, J. H.
Affiliations: SUNY Upstate Medical University (US)
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 2005-10
Volume: 280
Issue: 41
Pages: 34530-34537
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.m508890200
PMC: PMC1483127
OpenAlex: W2044025216
Cited by: 47
References: 67
Citations by year: 2025: 1 · 2024: 1 · 2021: 1 · 2020: 1 · 2019: 1 · 2018: 1 · 2017: 2 · 2016: 3 · 2015: 1 · 2013: 2 · 2012: 2
FWCI: 1.89
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 5466 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
Funders: National Institute of Diabetes and Digestive and Kidney Diseases (DK 49194, R01DK056294, R29DK049194, DK 56294, R01DK049194)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
Keywords: VCP, Ufd1, Npl4, IP3 receptor, ER-associated degradation, ubiquitin-proteasome system, receptor ubiquitination, proteasomal degradation, endothelin-1, calcium release, G protein-coupled receptor signaling
MeSH terms: Adenosine Triphosphatases, Animals, Calcium, Carrier Proteins, Cell Line, Cytosol, Electrophoresis, Polyacrylamide Gel, Endoplasmic Reticulum, Fibroblasts, Nuclear Proteins, Proteins, Subcellular Fractions, Time Factors, Calcium Channels, Down-Regulation, DNA, Complementary, Receptors, Cytoplasmic and Nuclear, Cell Cycle Proteins, Ubiquitin, RNA Interference, Intercellular Signaling Peptides and Proteins, Ubiquitin-Conjugating Enzymes, Immunoprecipitation, Intracellular Signaling Peptides and Proteins, Mice, Rats, Inositol 1,4,5-Trisphosphate Receptors

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Involvement of the p97-Ufd1-Npl4 Complex in the Regulated Endoplasmic Reticulum-associated Degradation of Inositol 1,4,5-Trisphosphate Receptors

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