ArticleAdvances in biological regulation2021
The Glo3 GAP crystal structure supports the molecular niche model for ArfGAPs in COPI coats.
Article in Advances in biological regulation, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 7 citations in OpenAlex.
- The Arf-GAP Age2 localizes to the late-Golgi via a conserved amphipathic helix.Molecular biology of the cell · 2023Article
- The Arf-GAP Age2 localizes to the late-Golgi via a conserved amphipathic helix.bioRxiv : the preprint server for biology · 2023Article
- An interaction between β'-COP and the ArfGAP, Glo3, maintains post-Golgi cargo recycling.The Journal of cell biology · 2023Article
- Proteomic Analysis Reveals Differential Expression Profiles in Idiopathic Pulmonary Fibrosis Cell Lines.International journal of molecular sciences · 2022Article
- An online gathering about the latest on molecular membrane biology.The Journal of biological chemistry · 2021Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Arf GTPase activating (ArfGAP) proteins are critical regulatory and effector proteins in membrane trafficking pathways. Budding yeast contain two ArfGAP proteins (Gcs1 and Glo3) implicated in COPI coat function at the Golgi, and yeast require Glo3 catalytic function for viability. A new X-ray crystal structure of the Glo3 GAP domain was determined at 2.1 Å resolution using molecular replacement methods. The structure reveals a Cys
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