ArticlePLoS biology2018
Surf4 (Erv29p) binds amino-terminal tripeptide motifs of soluble cargo proteins with different affinities, enabling prioritization of their exit from the endoplasmic reticulum.
Article in PLoS biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 78 citations in OpenAlex.
- Systematic optimization ofEngineering microbiology · 2026Review
- Beyond Vesicular Traffic: The ERES as the Gateway for Biosynthetic Secretion.Sub-cellular biochemistry · 2026Review
- 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
- A family study of dentinogenesis imperfecta shields type II caused by a novel DSPP mutation and investigations on the isolated stem cells from human exfoliated deciduous teeth.BMC oral health · 2025Article
- ER export via SURF4 uses diverse mechanisms of both client and coat engagement.The Journal of cell biology · 2025Article
- Inositol-requiring enzyme 1 alpha is essential for dentinogenesis.Frontiers in physiology · 2025Article
- LMAN1 serves as a cargo receptor for thrombopoietin.JCI insight · 2024Article
- Genetics of hemostasis: from bedside to bench and back again.The Journal of clinical investigation · 2024Article
- Surfeit locus protein 4 modulates endoplasmic reticulum function and maintains oocyte quality.Cell cycle (Georgetown, Tex.) · 2024Article
- VLDL Biogenesis and Secretion: It Takes a Village.Circulation research · 2024Review
- Conventional and Unconventional Protein Secretion in Yeast and Animal Cells.Methods in molecular biology (Clifton, N.J.) · 2024Review
- Identification of LMAN1- and SURF4-Dependent Secretory Cargoes.Journal of proteome research · 2023Article
- Mammalian cargo receptors for endoplasmic reticulum-to-Golgi transport: mechanisms and interactions.Biochemical Society transactions · 2023Review
- Cargo Receptor-Mediated ER Export in Lipoprotein Secretion and Lipid Homeostasis.Cold Spring Harbor perspectives in biology · 2023Review
- Dentin defects caused by a DsppScientific reports · 2023Article
- Surf4, cargo trafficking, lipid metabolism, and therapeutic implications.Journal of molecular cell biology · 2023Review
- Cargo selection in endoplasmic reticulum-to-Golgi transport and relevant diseases.The Journal of clinical investigation · 2023Review
- Hepatic inactivation of murineeLife · 2022Article
- Selective inhibition of protein secretion by abrogating receptor-coat interactions during ER export.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Translated MutantJournal of personalized medicine · 2022Article
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7 authors at 2 institutions in 1 country.
Funding
Abstract
Some secreted proteins that assemble into large complexes, such as extracellular matrices or hormones and enzymes in storage granules, must be kept at subaggregation concentrations during intracellular trafficking. We show surfeit locus protein 4 (Surf4) is the cargo receptor that establishes different steady-state concentrations for a variety of soluble cargo proteins within the endoplasmic reticulum (ER) through interaction with the amino-terminal tripeptides exposed after removal of leader sequences. We call this motif the ER-Exit by Soluble Cargo using Amino-terminal Peptide-Encoding motif (ER-ESCAPE motif). Proteins that most readily aggregate in the ER lumen (e.g., dentin sialophosphoprotein [DSPP] and amelogenin, X-linked [AMELX]) have strong ER-ESCAPE motifs to inhibit aggregate formation, while less susceptible cargo exhibits weaker motifs. Specific changes in a single amino acid of the tripeptide result in aggregate formation and failure to efficiently traffic cargo out of the ER. A logical subset of 8,000 possible tripeptides starting a model soluble cargo protein (growth hormone) established a continuum of steady-state ER concentrations ranging from low (i.e., high affinity for receptor) to the highest concentrations associated with bulk flow-limited trafficking observed for nonbinding motifs. Human cells lacking Surf4 no longer preferentially trafficked cargo expressing strong ER-ESCAPE motifs. Reexpression of Surf4 or expression of yeast's ortholog, ER-derived vesicles protein 29 (Erv29p), rescued enhanced ER trafficking in Surf4-null cells. Hence our work describes a new way of preferentially exporting soluble cargo out of the ER that maintains proteins below the concentrations at which they form damaging aggregates.
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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.