ArticleTraffic (Copenhagen, Denmark)2016
Human Peroxin PEX3 Is Co-translationally Integrated into the ER and Exits the ER in Budding Vesicles.
Article in Traffic (Copenhagen, Denmark), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
16 citing papers in PubMed.
- Mammalian pexophagy at a glance.Journal of cell science · 2024Review
- Quantitative Mass Spectrometry Characterizes Client Spectra of Components for Targeting of Membrane Proteins to and Their Insertion into the Membrane of the Human ER.International journal of molecular sciences · 2023Review
- The subset of peroxisomal tail-anchored proteins do not reach peroxisomes via ER, instead mitochondria can be involved.PloS one · 2023Article
- The Effect of aCells · 2022Article
- Signal Peptide Features Determining the Substrate Specificities of Targeting and Translocation Components in Human ER Protein Import.Frontiers in physiology · 2022Review
- Quantitative Proteomics and Differential Protein Abundance Analysis after the Depletion of PEX3 from Human Cells Identifies Additional Aspects of Protein Targeting to the ER.International journal of molecular sciences · 2021Article
- Glycosome heterogeneity in kinetoplastids.Biochemical Society transactions · 2021Review
- mRNA Targeting, Transport and Local Translation in Eukaryotic Cells: From the Classical View to a Diversity of New Concepts.Molecular biology · 2021Article
- Peroxisome prognostications: Exploring the birth, life, and death of an organelle.The Journal of cell biology · 2020Review
- Peroxisome biogenesis, membrane contact sites, and quality control.EMBO reports · 2019Review
- ESCRT-III is required for scissioning new peroxisomes from the endoplasmic reticulum.The Journal of cell biology · 2018Article
- Redox Regulation of Homeostasis and Proteostasis in Peroxisomes.Physiological reviews · 2018Review
- A New Yeast Peroxin, Pex36, a Functional Homolog of Mammalian PEX16, Functions in the ER-to-Peroxisome Traffic of Peroxisomal Membrane Proteins.Journal of molecular biology · 2017Article
- Article
- Peroxin-dependent targeting of a lipid-droplet-destined membrane protein to ER subdomains.Nature cell biology · 2016Article
- Peroxisome biogenesis and human peroxisome-deficiency disorders.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2016Review
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
The long-standing paradigm that all peroxisomal proteins are imported post-translationally into pre-existing peroxisomes has been challenged by the detection of peroxisomal membrane proteins (PMPs) inside the endoplasmic reticulum (ER). In mammals, the mechanisms of ER entry and exit of PMPs are completely unknown. We show that the human PMP PEX3 inserts co-translationally into the mammalian ER via the Sec61 translocon. Photocrosslinking and fluorescence spectroscopy studies demonstrate that the N-terminal transmembrane segment (TMS) of ribosome-bound PEX3 is recognized by the signal recognition particle (SRP). Binding to SRP is a prerequisite for targeting of the PEX3-containing ribosome•nascent chain complex (RNC) to the translocon, where an ordered multistep pathway integrates the nascent chain into the membrane adjacent to translocon proteins Sec61α and TRAM. This insertion of PEX3 into the ER is physiologically relevant because PEX3 then exits the ER via budding vesicles in an ATP-dependent process. This study identifies early steps in human peroxisomal biogenesis by demonstrating sequential stages of PMP passage through the mammalian ER.
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Registered trials
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.