ArticleProceedings of the National Academy of Sciences of the United States of America2016
δ-COP contains a helix C-terminal to its longin domain key to COPI dynamics and function.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 10 citations in OpenAlex.
- Identification of a Fetal De Novo Splice Variant inMaternal-fetal medicine (Wolters Kluwer Health, Inc.) · 2025Article
- From guide to guard-activation mechanism of the stress-sensing chaperone Get3.Molecular cell · 2022Article
- 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
- Dissection of GTPase-activating proteins reveals functional asymmetry in the COPI coat of budding yeast.Journal of cell science · 2019Article
- Article
- 9Å structure of the COPI coat reveals that the Arf1 GTPase occupies two contrasting molecular environments.eLife · 2017Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Membrane recruitment of coatomer and formation of coat protein I (COPI)-coated vesicles is crucial to homeostasis in the early secretory pathway. The conformational dynamics of COPI during cargo capture and vesicle formation is incompletely understood. By scanning the length of δ-COP via functional complementation in yeast, we dissect the domains of the δ-COP subunit. We show that the μ-homology domain is dispensable for COPI function in the early secretory pathway, whereas the N-terminal longin domain is essential. We map a previously uncharacterized helix, C-terminal to the longin domain, that is specifically required for the retrieval of HDEL-bearing endoplasmic reticulum-luminal residents. It is positionally analogous to an unstructured linker that becomes helical and membrane-facing in the open form of the AP2 clathrin adaptor complex. Based on the amphipathic nature of the critical helix it may probe the membrane for lipid packing defects or mediate interaction with cargo and thus contribute to stabilizing membrane-associated coatomer.
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