ArticlePloS one2012
Sec12 binds to Sec16 at transitional ER sites.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 54 citations in OpenAlex.
- Beyond Vesicular Traffic: The ERES as the Gateway for Biosynthetic Secretion.Sub-cellular biochemistry · 2026Review
- TFG regulates inner COPII coat recruitment to facilitate anterograde secretory protein transport.Molecular biology of the cell · 2024Article
- Knockdown of Sec16 causes early lethality and defective deposition of the protein Rp30 in the eggshell of the vectorFrontiers in cell and developmental biology · 2024Article
- ER exit in physiology and disease.Frontiers in molecular biosciences · 2024Review
- Nutrient deprivation alters the rate of COPII subunit recruitment at ER subdomains to tune secretory protein transport.Nature communications · 2023Article
- The Sar1 GTPase is dispensable for COPII-dependent cargo export from the ER.Cell reports · 2023Article
- Sec16 and Sed4 interdependently function as interaction and localization partners at ER exit sites.Journal of cell science · 2023Article
- Pathway engineering facilitates efficient protein expression in Pichia pastoris.Applied microbiology and biotechnology · 2022Review
- CRISPR/Cas9-mediated point mutations improve α-amylase secretion in Saccharomyces cerevisiae.FEMS yeast research · 2022Article
- ER arrival sites associate with ER exit sites to create bidirectional transport portals.The Journal of cell biology · 2020Article
- Dysregulated Plasma Membrane Turnover Underlying Dendritic Pathology in Neurodegenerative Diseases.Frontiers in cellular neuroscience · 2020Review
- LTK is an ER-resident receptor tyrosine kinase that regulates secretion.The Journal of cell biology · 2019Article
- COPII-mediated trafficking at the ER/ERGIC interface.Traffic (Copenhagen, Denmark) · 2019Review
- COPII vesicles can affect the activity of antisense oligonucleotides by facilitating the release of oligonucleotides from endocytic pathways.Nucleic acids research · 2018Article
- COPII-dependent ER export in animal cells: adaptation and control for diverse cargo.Histochemistry and cell biology · 2018Review
- Remodeling of ER-exit sites initiates a membrane supply pathway for autophagosome biogenesis.EMBO reports · 2017Article
- A Wntless-SEC12 complex on the ER membrane regulates early Wnt secretory vesicle assembly and mature ligand export.Journal of cell science · 2017Article
- TANGO1 recruits Sec16 to coordinately organize ER exit sites for efficient secretion.The Journal of cell biology · 2017Article
- Regulation of ER-Golgi Transport Dynamics by GTPases in Budding Yeast.Frontiers in cell and developmental biology · 2017Review
- Regulation of the Sar1 GTPase Cycle Is Necessary for Large Cargo Secretion from the Endoplasmic Reticulum.Frontiers in cell and developmental biology · 2017Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
COPII vesicles bud from an ER domain known as the transitional ER (tER). Assembly of the COPII coat is initiated by the transmembrane guanine nucleotide exchange factor Sec12. In the budding yeast Pichia pastoris, Sec12 is concentrated at tER sites. Previously, we found that the tER localization of P. pastoris Sec12 requires a saturable binding partner. We now show that this binding partner is Sec16, a peripheral membrane protein that functions in ER export and tER organization. One line of evidence is that overexpression of Sec12 delocalizes Sec12 to the general ER, but simultaneous overexpression of Sec16 retains overexpressed Sec12 at tER sites. Additionally, when P. pastoris Sec12 is expressed in S. cerevisiae, the exogenous Sec12 localizes to the general ER, but when P. pastoris Sec16 is expressed in the same cells, the exogenous Sec12 is recruited to tER sites. In both of these experimental systems, the ability of Sec16 to recruit Sec12 to tER sites is abolished by deleting a C-terminal fragment of Sec16. Biochemical experiments confirm that this C-terminal fragment of Sec16 binds to the cytosolic domain of Sec12. Similarly, we demonstrate that human Sec12 is concentrated at tER sites, likely due to association with a C-terminal fragment of Sec16A. These results suggest that a Sec12-Sec16 interaction has a conserved role in ER export.
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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.