ArticleProceedings of the National Academy of Sciences of the United States of America2024
Sec7 regulatory domains scaffold autoinhibited and active conformations.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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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
6 citing papers in PubMed, 5 citations in OpenAlex.
- An activating mutation in AGEF-1, a putative Arf GEF, causes yolk extrusion frombioRxiv : the preprint server for biology · 2026Article
- An activating mutation in AGEF-1, a putative Arf GEF, causes yolk extrusion frommicroPublication biology · 2026Article
- Structural insights into traffic through the Golgi complex.Current opinion in cell biology · 2025Review
- Structural basis for Rab6 activation by the Ric1-Rgp1 complex.Nature communications · 2024Article
- Structural basis for Rab6 activation by the Ric1-Rgp1 complex.bioRxiv : the preprint server for biology · 2024Article
- Structural insight into an Arl1-ArfGEF complex involved in Golgi recruitment of a GRIP-domain golgin.Nature communications · 2024Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The late stages of Golgi maturation involve a series of sequential trafficking events in which cargo-laden vesicles are produced and targeted to multiple distinct subcellular destinations. Each of these vesicle biogenesis events requires activation of an Arf GTPase by the Sec7/BIG guanine nucleotide exchange factor (GEF). Sec7 localization and activity is regulated by autoinhibition, positive feedback, and interaction with other GTPases. Although these mechanisms have been characterized biochemically, we lack a clear picture of how GEF localization and activity is modulated by these signals. Here, we report the cryogenic electron microscopy structure of full-length Sec7 in its autoinhibited form, revealing the architecture of its multiple regulatory domains. We use functional experiments to determine the basis for autoinhibition and use structural predictions to produce a model for an active conformation of the GEF that is supported empirically. This study therefore elucidates the conformational transition that Sec7 undergoes to become active on the organelle membrane surface.
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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 Socratic graph.