ArticlePloS one2011
The tissue-specific Rep8/UBXD6 tethers p97 to the endoplasmic reticulum membrane for degradation of misfolded proteins.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 15 citations in OpenAlex.
- A Prognostic Nomogram Based on an Immunogenic Cell Death and Endoplasmic Reticulum Stress-Related Gene Signature for Ovarian Cancer.International journal of women's health · 2025Article
- Generation of chimeric antigen receptor T cells targeting p95HER2 in solid tumors.Nature communications · 2024Article
- Exploring the role of ubiquitin regulatory X domain family proteins in cancers: bioinformatics insights, mechanisms, and implications for therapy.Journal of translational medicine · 2024Review
- UBXD8 mediates mitochondria-associated degradation to restrain apoptosis and mitophagy.EMBO reports · 2022Article
- A Mighty "Protein Extractor" of the Cell: Structure and Function of the p97/CDC48 ATPase.Frontiers in molecular biosciences · 2017Review
- UBXD Proteins: A Family of Proteins with Diverse Functions in Cancer.International journal of molecular sciences · 2016Review
- Systematic proteomics of the VCP-UBXD adaptor network identifies a role for UBXN10 in regulating ciliogenesis.Nature cell biology · 2015Article
- Human ASPL/TUG interacts with p97 and complements the proteasome mislocalization of a yeast ubx4 mutant, but not the ER-associated degradation defect.BMC cell biology · 2014Article
- The intrinsically disordered membrane protein selenoprotein S is a reductase in vitro.Biochemistry · 2013Article
- Distribution of the SELMA translocon in secondary plastids of red algal origin and predicted uncoupling of ubiquitin-dependent translocation from degradation.Eukaryotic cell · 2012Article
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Authors and funding
9 authors at 6 institutions in 4 countries.
Funding
Abstract
The protein known as p97 or VCP in mammals and Cdc48 in yeast is a versatile ATPase complex involved in several biological functions including membrane fusion, protein folding, and activation of membrane-bound transcription factors. In addition, p97 plays a central role in degradation of misfolded secretory proteins via the ER-associated degradation pathway. This functional diversity of p97 depends on its association with various cofactors, and to further our understanding of p97 function it is important that these cofactors are identified and analyzed. Here, we isolate and characterize the human protein named Rep8 or Ubxd6 as a new cofactor of p97. Mouse Rep8 is highly tissue-specific and abundant in gonads. In testes, Rep8 is expressed in post-meiotic round spermatids, whereas in ovaries Rep8 is expressed in granulosa cells. Rep8 associates directly with p97 via its UBX domain. We show that Rep8 is a transmembrane protein that localizes to the ER membrane with its UBX domain facing the cytoplasm. Knock-down of Rep8 expression in human cells leads to a decreased association of p97 with the ER membrane and concomitantly a retarded degradation of misfolded ER-derived proteasome substrates. Thus, Rep8 tethers p97 to the ER membrane for efficient ER-associated degradation.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.