ArticleBMC genomics2005
The domain architecture of large guanine nucleotide exchange factors for the small GTP-binding protein Arf.
Article in BMC genomics, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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Who cites it
52 citing papers in PubMed, 108 citations in OpenAlex.
- BsSYT1 is required for growth, conidiogenesis, stress response and virulence of Bipolaris sorokiniana.World journal of microbiology & biotechnology · 2026Article
- TBC9, an essential TBC-domain protein, regulates early vesicular transport and IMC formation in Toxoplasma gondii.Communications biology · 2024Article
- Systematic characterization of all Toxoplasma gondii TBC domain-containing proteins identifies an essential regulator of Rab2 in the secretory pathway.PLoS biology · 2024Article
- Sec7 regulatory domains scaffold autoinhibited and active conformations.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Structural insight into an Arl1-ArfGEF complex involved in Golgi recruitment of a GRIP-domain golgin.Nature communications · 2024Article
- Kinetics of Arf1 inactivation regulates Golgi organisation and function in non-adherent fibroblasts.Biology open · 2023Article
- The Arf-GEF GBF1 undergoes multi-domain structural shifts to activate Arf at the Golgi.Frontiers in cell and developmental biology · 2023Article
- Article
- Structural basis for activation of Arf1 at the Golgi complex.Cell reports · 2022Article
- Modeling the dynamic behaviors of the COPI vesicle formation regulators, the small GTPase Arf1 and its activating Sec7 guanine nucleotide exchange factor GBF1 on Golgi membranes.Molecular biology of the cell · 2021Article
- Single Amino Acid Exchange in ACTIN2 Confers Increased Tolerance to Oxidative Stress in ArabidopsisInternational journal of molecular sciences · 2021Article
- Ancient complement and lineage-specific evolution of the Sec7 ARF GEF proteins in eukaryotes.Molecular biology of the cell · 2019Article
- ARF GTPases and their GEFs and GAPs: concepts and challenges.Molecular biology of the cell · 2019Review
- PH-domain-binding inhibitors of nucleotide exchange factor BRAG2 disrupt Arf GTPase signaling.Nature chemical biology · 2019Article
- Nonselective Chemical Inhibition of Sec7 Domain-Containing ARF GTPase Exchange Factors.The Plant cell · 2018Article
- The Arf-GDP-regulated recruitment of GBF1 to Golgi membranes requires domains HDS1 and HDS2 and a Golgi-localized protein receptor.Journal of cell science · 2018Article
- The Arf GEF GBF1 and Arf4 synergize with the sensory receptor cargo, rhodopsin, to regulate ciliary membrane trafficking.Journal of cell science · 2017Article
- Regulation of Arf activation occurs via distinct mechanisms at early and late Golgi compartments.Molecular biology of the cell · 2017Article
- Impairment of Cargo Transportation Caused byThe Journal of biological chemistry · 2017Article
- Allosteric regulation of Arf GTPases and their GEFs at the membrane interface.Small GTPases · 2016Review
Corrections and comments
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Authors and funding
9 authors at 6 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundSmall G proteins, which are essential regulators of multiple cellular functions, are activated by guanine nucleotide exchange factors (GEFs) that stimulate the exchange of the tightly bound GDP nucleotide by GTP. The catalytic domain responsible for nucleotide exchange is in general associated with non-catalytic domains that define the spatio-temporal conditions of activation. In the case of small G proteins of the Arf subfamily, which are major regulators of membrane trafficking, GEFs form a heterogeneous family whose only common characteristic is the well-characterized Sec7 catalytic domain. In contrast, the function of non-catalytic domains and how they regulate/cooperate with the catalytic domain is essentially unknown.
resultsBased on Sec7-containing sequences from fully-annotated eukaryotic genomes, including our annotation of these sequences from Paramecium, we have investigated the domain architecture of large ArfGEFs of the BIG and GBF subfamilies, which are involved in Golgi traffic. Multiple sequence alignments combined with the analysis of predicted secondary structures, non-structured regions and splicing patterns, identifies five novel non-catalytic structural domains which are common to both subfamilies, revealing that they share a conserved modular organization. We also report a novel ArfGEF subfamily with a domain organization so far unique to alveolates, which we name TBS (TBC-Sec7).
conclusionOur analysis unifies the BIG and GBF subfamilies into a higher order subfamily, which, together with their being the only subfamilies common to all eukaryotes, suggests that they descend from a common ancestor from which species-specific ArfGEFs have subsequently evolved. Our identification of a conserved modular architecture provides a background for future functional investigation of non-catalytic domains.
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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.