ArticleMolecular biology of the cell2020
ESCargo: a regulatable fluorescent secretory cargo for diverse model organisms.
Article in Molecular biology of the cell, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 21 citations in OpenAlex.
- SNX6-mediated subunit-specific secretory trafficking of AMPA receptors regulates synaptic function and plasticity.Communications biology · 2025Article
- The secretory pathway in Tetrahymena is organized for efficient constitutive secretion at ciliary pockets.iScience · 2024Article
- Nutrient deprivation alters the rate of COPII subunit recruitment at ER subdomains to tune secretory protein transport.Nature communications · 2023Article
- CRISPR/Cas9-mediated point mutations improve α-amylase secretion in Saccharomyces cerevisiae.FEMS yeast research · 2022Article
- Bioorthogonal, Fluorogenic Targeting of Voltage-Sensitive Fluorophores for Visualizing Membrane Potential Dynamics in Cellular Organelles.Journal of the American Chemical Society · 2022Article
- Genetically encoded fluorescent tools: Shining a little light on ER-to-Golgi transport.Free radical biology & medicine · 2022Review
- SURF4-induced tubular ERGIC selectively expedites ER-to-Golgi transport.Developmental cell · 2022Article
- Activity-dependent Golgi satellite formation in dendrites reshapes the neuronal surface glycoproteome.eLife · 2021Article
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
Abstract
Membrane traffic can be studied by imaging a cargo protein as it transits the secretory pathway. The best tools for this purpose initially block export of the secretory cargo from the endoplasmic reticulum (ER) and then release the block to generate a cargo wave. However, previously developed regulatable secretory cargoes are often tricky to use or specific for a single model organism. To overcome these hurdles for budding yeast, we recently optimized an artificial fluorescent secretory protein that exits the ER with the aid of the Erv29 cargo receptor, which is homologous to mammalian Surf4. The fluorescent secretory protein forms aggregates in the ER lumen and can be rapidly disaggregated by addition of a ligand to generate a nearly synchronized cargo wave. Here we term this regulatable secretory protein ESCargo (Erv29/Surf4-dependent secretory cargo) and demonstrate its utility not only in yeast cells, but also in cultured mammalian cells,
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