Ask about this productRelated genes to: GBF1 (1844) antibody
- Gene:
- GBF1 NIH gene
- Name:
- golgi brefeldin A resistant guanine nucleotide exchange factor 1
- Previous symbol:
- -
- Synonyms:
- KIAA0248, ARF1GEF
- Chromosome:
- 10q24.32
- Locus Type:
- gene with protein product
- Date approved:
- 1999-01-14
- Date modifiied:
- 2016-10-05
Related products to: GBF1 (1844) antibody
Related articles to: GBF1 (1844) antibody
- The armadillo repeat protein ARMH3 regulates the activity and localization of the Golgi resident lipid kinase phosphatidylinositol 4 kinase IIIβ (PI4KB) and the Golgi-specific brefeldin A-resistance guanine nucleotide exchange factor 1 (GBF1) that activates Arf1. ARMH3 localizes to the trans-Golgi network (TGN) via the GTPase Arl5. We used hydrogen deuterium exchange mass spectrometry (HDX-MS) and AI-enabled modeling to define the interfaces of ARMH3 with its binding partners Arl5, PI4KB, and GBF1. The ARMH3-Arl5 interface was determined to consist of regions near the N and C termini of ARMH3, with Arl5 binding causing allosteric conformational changes in ARMH3 located at a shared PI4KB/GBF1 interface. ARMH3 binds to PI4KB and GBF1 at this shared competitive interface, with GBF1 binding to ARMH3 through a disordered loop we have named the ARMH3-binding region (ABR). Both GBF1 and PI4KB can form ternary complexes with ARMH3-Arl5. The ARMH3 interfaces in PI4KB and GBF1 contain phosphosites, with the phosphomimetic mutation of GBF1 blocking complex formation. These findings provide new insights into the role of ARMH3 as a master coordinator of GTPase and phosphoinositide signaling at the Golgi/TGN. - Source: PubMed
Publication date: 2026/06/29
Scott Mackenzie KKlynsoon Giselle C TWalsh Emma ESuresh SushantNyvall Hunter GBurke John E - Reactive oxygen species (ROS) are pivotal signals that trigger the transition from seed dormancy to germination, yet the molecular link between ROS and transcriptional regulation has remained unclear. Here, we uncover a redox-dependent mechanism focusing on the transcription factor G-box binding factor 1 (GBF1) and its chaperone GBF1-interacting protein 1 (GIP1). We show that GBF1 undergoes liquid-liquid phase separation (LLPS) to form condensates that enhance target DNA binding and repress the transcription of the germination-promoting gene Cathepsin B-like protease 3 (CathB3). Both the prion-like domain and the bZIP dimerization domain are indispensable for GBF1 condensation and DNA binding. GIP1 colocalizes with GBF1 and functions as a molecular chaperone that fine-tunes condensate size and liquidity, thereby enhancing GBF1's DNA-binding and repressive capacity. Oxidation of GIP1 by ROS burst during germination abolishes its chaperone activity, leading to aberrant, less dynamic GBF1 condensates and consequent derepression of CathB3, which promotes germination. This work identifies a ROS-sensitive chaperone-condensate axis as a key molecular gatekeeper of seed germination, revealing how redox signals are translated into developmental decisions through the material properties of transcriptional condensates. - Source: PubMed
Publication date: 2026/05/26
Wang YunyingFang Xiaofeng - Cell-matrix adhesion regulates membrane trafficking, Golgi organization, and function. Altered Golgi organization in cancer cells may influence trafficking and cargo processing. A simple screen revealed distinct, adhesion-dependent differences in Golgi organization across breast (MDAMB231 versus MCF7) and lung (A549 versus CaLu1) cancer cell lines. To identify regulators driving these differences, we performed an in silico analysis of differentially expressed genes in the Cancer Cell Line Encyclopedia dataset, integrating Golgi-associated functions from interaction networks and literature. This analysis highlighted AXL as a putative Golgi regulator. AXL is prominently localized to the Golgi and is displaced upon inhibition with R428, which disrupts Golgi organization. AXL knockdown also does the same. AXL-mediated regulation of the Golgi is adhesion dependent. Mechanistically, AXL controls Arf1 activation through an AMPK-GBF1 pathway. Targeting of AMPK activation thus significantly reverses R428-mediated Golgi disorganization. Loss of adhesion promotes AMPK and reduces Arf1 activity, displacing AXL and Arf1 from the Golgi, driving its disorganization. This impacts Golgi-associated functions, tubulin acetylation in MDAMB231 cells, and cell-surface glycosylation in A549 cells. Together, our findings identify an adhesion-AXL-AMPK-GBF1-Arf1 pathway governing Golgi organization and function in cancer cells. - Source: PubMed
Publication date: 2026/05/19
Joshi PrachiSaha ArnavMalaviya RadhikaPanda DebiprasadMehta GrishmaPattanayak ManojeetSingh VibhaBalasubramanian Nagaraj - Despite the identification of familial Alzheimer's disease (FAD) genes and neuropathological alterations, AD displays complex genetic heterogeneity and molecular pathogenesis that warrant further investigation. GBF1 (Golgi brefeldin A resistant guanine nucleotide exchange factor 1) regulates protein trafficking, and genetic variants of GBF1 are associated with axonal neuropathy, intelligence, and cognitive function. - Source: PubMed
Miller Sean JProkopenko DmitryBai PingMondal PrasenjitScott AbigaelZhang WeiGomm AshleyZhang SiyiChild Daniel DShen NolanWard JosephSchulte ScottLei DanHafler Brian PWang ChangningTanzi Rudolph EZhang Can - Influenza viruses and severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) are respiratory pathogens that continue to challenge global health due to their efficient transmission and ability to circumvent virus-specific treatments. Targeting host factors that are essential for viral replication may enable the development of broad-spectrum antivirals with reduced resistance potential. Here, we used small interfering RNA (siRNA) to screen 91 host factors previously implicated in influenza virus replication and identified seven that were also required for SARS-CoV-2 replication. Of these, Golgi-specific brefeldin A-resistance factor 1 (GBF1), a guanine nucleotide exchange factor involved in coat protein complex I (COPI) vesicle trafficking, was also involved in human coronavirus 229E replication. We found that GBF1 relocated to sites of viral replication in SARS-CoV-2-infected cells. Using a computational design pipeline, we generated antisense oligonucleotides (ASOs) targeting GBF1. The lead candidate, GBF1-ASO#1502, potently inhibited influenza viruses and SARS-CoV-2 , with nanomolar half-maximal inhibitory concentration (IC) values and favorable selectivity indices. GBF1-targeting ASOs thus represent a promising host-directed antiviral approach for controlling respiratory RNA viruses. - Source: PubMed
Publication date: 2026/01/29
Simanihuruk VictoriaKida YurieTakada KosukeYamaguma HarumiKameoka NatsumiAnzai ItsukiShichinohe ShintaroObika SatoshiKasahara YuuyaWatanabe Tokiko