ArticleMolecular biology of the cell2004
Endoplasmic reticulum quality control of unassembled iron transporter depends on Rer1p-mediated retrieval from the golgi.
Article in Molecular biology of the cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 53 citations in OpenAlex.
- The Erv41-Erv46 complex serves as a retrograde receptor to retrieve misfolded secretory proteins that have escaped from the ER.Molecular biology of the cell · 2025Article
- Different Proteostasis Mechanisms Facilitate the Assembly of Individual Components on the Chitin Synthase 3 Complex at the Endoplasmic Reticulum.Journal of fungi (Basel, Switzerland) · 2025Article
- The Ferroxidase-Permease System for Transport of Iron Across Membranes: From Yeast to Humans.International journal of molecular sciences · 2025Review
- DAP12 interacts with RER1 and is retained in the secretory pathway before assembly with TREM2.Cellular and molecular life sciences : CMLS · 2024Article
- Maintenance of proteostasis by Drosophila Rer1 is essential for competitive cell survival and Myc-driven overgrowth.PLoS genetics · 2024Article
- The protein kinase Ire1 has a Hac1-independent essential role in iron uptake and virulence of Candida albicans.PLoS pathogens · 2022Article
- Protein folding state-dependent sorting at the Golgi apparatus.Molecular biology of the cell · 2019Article
- Rer1-mediated quality control system is required for neural stem cell maintenance during cerebral cortex development.PLoS genetics · 2018Article
- The Incomplete Glutathione Puzzle: Just Guessing at Numbers and Figures?Antioxidants & redox signaling · 2017Review
- Neurodegeneration-associated mutant TREM2 proteins abortively cycle between the ER and ER-Golgi intermediate compartment.Molecular biology of the cell · 2017Article
- Two novel effectors of trafficking and maturation of the yeast plasma membrane HTraffic (Copenhagen, Denmark) · 2017Article
- Protein sorting at the ER-Golgi interface.The Journal of cell biology · 2016Review
- Potassium and the K+/H+ Exchanger Kha1p Promote Binding of Copper to ApoFet3p Multi-copper Ferroxidase.The Journal of biological chemistry · 2016Article
- Rer1 and calnexin regulate endoplasmic reticulum retention of a peripheral myelin protein 22 mutant that causes type 1A Charcot-Marie-Tooth disease.Scientific reports · 2014Article
- Rer1p regulates the ER retention of immature rhodopsin and modulates its intracellular trafficking.Scientific reports · 2014Article
- Conduits of life's spark: a perspective on ion channel research since the birth of neuron.Neuron · 2013Review
- Anchors aweigh: protein localization and transport mediated by transmembrane domains.Trends in cell biology · 2013Review
- Rer1p maintains ciliary length and signaling by regulating γ-secretase activity and Foxj1a levels.The Journal of cell biology · 2013Article
- Protein quality control by Rer1p in the early secretory pathway: from mechanism to implication in Alzheimer's disease.Alzheimer's research & therapy · 2013Review
- Functional characterization of the ferroxidase, permease high-affinity iron transport complex from Candida albicans.Molecular microbiology · 2011Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Endoplasmic reticulum (ER) quality control is a conserved process by which misfolded or unassembled proteins are selectively retained in the endoplasmic reticulum (ER). Failure in oligomerization of multisubunit membrane proteins is one of the events that triggers ER quality control. The transmembrane domains (TMDs) of unassembled subunits are determinants of ER retention in many cases, although the mechanism of the TMD-mediated sorting of unassembled subunits remains elusive. We studied a yeast iron transporter complex on the cell surface as a new model system for ER quality control. When Fet3p, a transmembrane subunit, is not assembled with the other membrane subunit, Ftr1p, unassembled Fet3p is exclusively localized to the ER at steady state. The TMD of Fet3p contains a determinant for this process. However, pulse-chase analysis and in vitro budding assays indicate that unassembled Fet3p rapidly escapes from the ER. Furthermore, Rer1p, a retrieval receptor for ER-resident membrane proteins in the Golgi, is responsible for the TMD-dependent ER retrieval of unassembled Fet3p. These findings provide clear evidence that the ER quality control of unassembled membrane proteins can be achieved by retrieval from the Golgi and that Rer1p serves as a specific sorting receptor in this process.
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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.