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An interaction between β’-COP and the ArfGAP, Glo3, maintains post-Golgi cargo recycling
Open accessPreprint — published as 10.1083/jcb.202008061 · Paper page
Abstract
The essential COPI vesicular coat mediates retrieval of key transmembrane proteins at the Golgi and endosomes following recruitment by the small GTPase, Arf1. ArfGAP proteins regulate COPI coats, but molecular details for COPI recognition by ArfGAP proteins remain elusive. Biochemical and biophysical data reveal how β’-COP propeller domains directly engage the yeast ArfGAP, Glo3, with a low micromolar binding affinity (K D ~1 µM). Calorimetry data demonstrate both β’-COP propeller domains are required to bind Glo3 using electrostatic interactions. An acidic patch on β’-COP (D437/D450) interacts with Glo3 lysine residues located within the BoCCS (Binding of Coatomer, Cargo, and SNAREs) region. Targeted point mutations in either Glo3 BoCCS or β’-COP abrogate the interaction in vitro , and loss of the β’-COP/Glo3 interaction drives Ste2 mis-sorting to the vacuole and aberrant Golgi morphology in budding yeast. Together, these data suggest cells require the β’-COP/Glo3 interaction for cargo recycling via endosomes and the TGN, where β’-COP may serve as a molecular platform to coordinate binding to multiple protein partners, including Glo3, Arf1, and the COPI F-subcomplex.
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Metadata
- Authors
- Xie, B., Guillem, C., Jung, C., Kendall, A. K., Date, S., Best, J. T., Graham, T. R., & Jackson, L. P.
- Affiliations
- Vanderbilt University (US)
- Corresponding author
- Jackson, Lauren P.
- ORCID
- Venue
- The Journal of Cell Biology
- Publisher
- openRxiv
- Published
- 2022-05-26
- Volume
- 222
- Issue
- 4
- ISSN
- 0021-9525 (ISSN-L)
- PMC
- PMC9960064
- OpenAlex
- W4321492109
- Cited by
- 6
- References
- 1
- Citations by year
- 2026: 4 · 2025: 1 · 2023: 1
- FWCI
- 0.86
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Cell Biology (publishedVersion, cc-by-nc-sa)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Funders
- Pew Charitable Trusts
- National Institutes of Health
- National Institute of General Medical Sciences (T32GM008320, R01GM118452, R35GM119525, R35GM144123)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Keywords
- beta-COP, ArfGAP, COPI coat, Arf1, protein-protein interaction, endosomes, trans-Golgi network, Golgi morphology, Saccharomyces cerevisiae
- MeSH terms
- Golgi Apparatus, Saccharomyces cerevisiae, GTPase-Activating Proteins, Coat Protein Complex I, Coatomer Protein, ADP-Ribosylation Factor 1, Saccharomyces cerevisiae Proteins, SNARE Proteins
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