ArticleMicrobial cell factories2014
Secretion of a foreign protein from budding yeasts is enhanced by cotranslational translocation and by suppression of vacuolar targeting.
Article in Microbial cell factories, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.
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67 citing papers in PubMed, 149 citations in OpenAlex.
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- Dual-channel optogenetics in yeast for multiplexed light-based control of cellular processes and pathways.Nature communications · 2026Article
- Functional assignment of Golgi-associated vesicle tethers to specific membrane recycling pathways.bioRxiv : the preprint server for biology · 2026Article
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- Engineering Saccharomyces cerevisiae secretory system for recombinant protein production: strategies from signal peptides to protease control.Archives of microbiology · 2026Review
- Enhanced secretion of thermostable phytases from Myceliophthora thermophila by Komagataella phaffii.Microbial cell factories · 2026Article
- An integrated cell and medium engineering approach for production of a nanobody fusion in Saccharomyces cerevisiae.Applied microbiology and biotechnology · 2026Article
- A chimeric rather than native secretion signal elicits stress-related transcriptional adaption during 75k γ-secalin production inFEMS microbes · 2026Article
- Engineering small peptide secretion inFrontiers in bioengineering and biotechnology · 2026Article
- High-level expression of zearalenone lactonohydrolase ZenG in Pichia pastoris via combinatorial strategy.Archives of microbiology · 2025Article
- PIONEER: A Periplasmic Display Platform for Synthetic Biology-Based Screening of Genetically Encoded Protein Regulators.bioRxiv : the preprint server for biology · 2025Article
- COPI-dependent intra-Golgi recycling at an intermediate stage of cisternal maturation.bioRxiv : the preprint server for biology · 2025Article
- Higher induction temperatures and the native secretion signal peptide promote rye prolamin 75k γ-secalin production in Komagataella phaffii.Microbial cell factories · 2025Article
- The MFα signal sequence in yeast-based protein secretion: challenges and innovations'.Applied microbiology and biotechnology · 2025Review
- Different results despite high homology: Comparative expression of human and murine DNase1 in Pichia pastoris.PloS one · 2025Article
- Unlocking the power of antimicrobial peptides: advances in production, optimization, and therapeutics.Frontiers in cellular and infection microbiology · 2025Review
- Engineering protein translocation and unfolded protein response enhanced human PH-20 secretion in Pichia pastoris.Applied microbiology and biotechnology · 2024Article
- Recombinant production of Paenibacillus wynnii β-galactosidase with Komagataella phaffii.Microbial cell factories · 2024Article
7 more citing papers are in PubMed but not listed here.
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2 authors at 1 institution in 1 country.
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Abstract
backgroundBudding yeasts are often used to secrete foreign proteins, but the efficiency is variable. To identify roadblocks in the yeast secretory pathway, we used a monomeric superfolder GFP (msGFP) as a visual tracer in Saccharomyces cerevisiae and Pichia pastoris.
resultsOne roadblock for msGFP secretion is translocation into the ER. Foreign proteins are typically fused to the bipartite α-factor secretion signal, which consists of the signal sequence followed by the pro region. The α-factor signal sequence directs posttranslational translocation. For msGFP, posttranslational translocation is inefficient with the α-factor signal sequence alone but is stimulated by the pro region. This requirement for the pro region can be bypassed by using the Ost1 signal sequence, which has been shown to direct cotranslational translocation. A hybrid secretion signal consisting of the Ost1 signal sequence followed by the α-factor pro region drives efficient translocation followed by rapid ER export. A second roadblock for msGFP secretion in S. cerevisiae occurs during exit from the Golgi, when some of the msGFP molecules are diverted to the vacuole. Deletion of the sorting receptor Vps10 prevents vacuolar targeting of msGFP at the expense of missorting vacuolar hydrolases such as carboxypeptidase Y (CPY) to the culture medium. However, a truncation of Vps10 blocks vacuolar targeting of msGFP while permitting CPY to be sorted normally.
conclusionsWith budding yeasts, if the secretion or processing of a foreign protein is poor, we recommend two options. First, use the Ost1 signal sequence to achieve efficient entry into the secretory pathway while avoiding the processing issues associated with the α-factor pro region. Second, truncate Vps10 to suppress diversion to the vacuole. These insights obtained with msGFP highlight the value of applying cell biological methods to study yeast secretion.
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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.