ArticleScientific reports2018
The peroxisome biogenesis factors posttranslationally target reticulon homology domain-containing proteins to the endoplasmic reticulum membrane.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- Navigating lipid droplet proteins - part I: ER targeting routes of lipid droplet-destined membrane proteins.Biochemical Society transactions · 2025Review
- Rules of Engagement for Components of Membrane Protein Biogenesis at the Human Endoplasmic Reticulum.International journal of molecular sciences · 2025Review
- ADP ribosylation factor-like GTPase 6-interacting protein 5 (Arl6IP5) is an ER membrane-shaping protein that modulates ER-phagy.The Journal of biological chemistry · 2025Article
- 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
- Proteomics Identifies Substrates and a Novel Component in hSnd2-Dependent ER Protein Targeting.Cells · 2022Article
- Co-translational biogenesis of lipid droplet integral membrane proteins.Journal of cell science · 2022Article
- Signal Peptide Features Determining the Substrate Specificities of Targeting and Translocation Components in Human ER Protein Import.Frontiers in physiology · 2022Review
- PEX19 Coordinates Neutral Lipid Storage in Cells in a Peroxisome-Independent Fashion.Frontiers in cell and developmental biology · 2022Article
- Dysfunctional peroxisomal lipid metabolisms and their ocular manifestations.Frontiers in cell and developmental biology · 2022Review
- Sharing the wealth: The versatility of proteins targeted to peroxisomes and other organelles.Frontiers in cell and developmental biology · 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
- Quantitative Proteomics and Differential Protein Abundance Analysis after Depletion of Putative mRNA Receptors in the ER Membrane of Human Cells Identifies Novel Aspects of mRNA Targeting to the ER.Molecules (Basel, Switzerland) · 2021Article
- Complexity and Specificity of Sec61-Channelopathies: Human Diseases Affecting Gating of the Sec61 Complex.Cells · 2021Review
- The Arabidopsis Plastidial Glucose-6-Phosphate Transporter GPT1 is Dually Targeted to Peroxisomes via the Endoplasmic Reticulum.The Plant cell · 2020Article
- Peroxisome prognostications: Exploring the birth, life, and death of an organelle.The Journal of cell biology · 2020Review
- The Oxymonad Genome Displays Canonical Eukaryotic Complexity in the Absence of a Mitochondrion.Molecular biology and evolution · 2019Article
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The endoplasmic reticulum (ER) is shaped by a class of membrane proteins containing reticulon homology domain (RHD), the conserved hydrophobic domain encompassing two short hairpin transmembrane domains. RHD resides in the outer leaflet of the ER membrane, generating high-curvature ER membrane. While most of the membrane proteins destined to enter the secretory pathway are cotranslationally targeted and inserted into ER membrane, the molecular mechanism how the RHD-containing proteins are targeted and inserted into the ER membrane remains to be clarified. Here we show that RHD-containing proteins can be posttranslationally targeted to the ER membrane. PEX19, a cytosolic peroxin, selectively recognizes the nascent RHD-containing proteins and mediates their posttranslational targeting in cooperation with PEX3, a membrane peroxin. Thus, these peroxisome biogenesis factors provide an alternative posttranslational route for membrane insertion of the RHD-containing proteins, implying that ER membrane shaping and peroxisome biogenesis may be coordinated by the posttranslational membrane insertion.
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