ArticleProceedings of the National Academy of Sciences of the United States of America2019
Roles of singleton tryptophan motifs in COPI coat stability and vesicle tethering.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed, 14 citations in OpenAlex.
- Tepsin binds LC3B to promote ATG9A trafficking and delivery.Molecular biology of the cell · 2024Article
- Structure of a membrane tethering complex incorporating multiple SNAREs.Nature structural & molecular biology · 2024Article
- Heterozygous mutations in the C-terminal domain of COPA underlie a complex autoinflammatory syndrome.The Journal of clinical investigation · 2024Article
- The machinery of vesicle fusion.Current opinion in cell biology · 2023Review
- Exploration of the Strategy for Improving the Expression of Heterologous Sweet Protein Monellin inJournal of fungi (Basel, Switzerland) · 2023Article
- Structural basis for the binding of SNAREs to the multisubunit tethering complex Dsl1.The Journal of biological chemistry · 2020Article
- Roles of singleton tryptophan motifs in COPI coat stability and vesicle tethering.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Coat protein I (COPI)-coated vesicles mediate retrograde transport from the Golgi to the endoplasmic reticulum (ER), as well as transport within the Golgi. Major progress has been made in defining the structure of COPI coats, in vitro and in vivo, at resolutions as high as 9 Å. Nevertheless, important questions remain unanswered, including what specific interactions stabilize COPI coats, how COPI vesicles recognize their target membranes, and how coat disassembly is coordinated with vesicle fusion and cargo delivery. Here, we use X-ray crystallography to identify a conserved site on the COPI subunit α-COP that binds to flexible, acidic sequences containing a single tryptophan residue. One such sequence, found within α-COP itself, mediates α-COP homo-oligomerization. Another such sequence is contained within the lasso of the ER-resident Dsl1 complex, where it helps mediate the tethering of Golgi-derived COPI vesicles at the ER membrane. Together, our findings suggest that α-COP homo-oligomerization plays a key role in COPI coat stability, with potential implications for the coordination of vesicle tethering, uncoating, and fusion.
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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.