ArticleAmerican journal of physiology. Cell physiology2016
Oligomerization of the Sec7 domain Arf guanine nucleotide exchange factor GBF1 is dispensable for Golgi localization and function but regulates degradation.
Article in American journal of physiology. Cell physiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 21 citations in OpenAlex.
- The lipid flippase ATP8A1 regulates the recruitment of ARF effectors to the trans-Golgi Network.Archives of biochemistry and biophysics · 2024Article
- Structural insight into an Arl1-ArfGEF complex involved in Golgi recruitment of a GRIP-domain golgin.Nature communications · 2024Article
- Site-specific phosphorylations of the Arf activator GBF1 differentially regulate GBF1 function in Golgi homeostasis and secretion versus cytokinesis.Scientific reports · 2023Article
- The Arf-GEF GBF1 undergoes multi-domain structural shifts to activate Arf at the Golgi.Frontiers in cell and developmental biology · 2023Article
- Structural basis for activation of Arf1 at the Golgi complex.Cell reports · 2022Article
- Article
- 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
- De Novo and Inherited Variants in GBF1 are Associated with Axonal Neuropathy Caused by Golgi Fragmentation.American journal of human genetics · 2020Article
- The Guanine Nucleotide Exchange Factor GBF1 Participates in Rotavirus Replication.Journal of virology · 2019Article
- Highly conserved motifs within the large Sec7 ARF guanine nucleotide exchange factor GBF1 target it to the Golgi and are critical for GBF1 activity.American journal of physiology. Cell physiology · 2018Article
- The HUS box is required for allosteric regulation of the Sec7 Arf-GEF.The Journal of biological chemistry · 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 guanine nucleotide exchange factor GBF1 is targeted to Golgi membranes through a PIP-binding domain.Journal of cell science · 2018Article
- Regulation of Arf activation occurs via distinct mechanisms at early and late Golgi compartments.Molecular biology of the cell · 2017Article
- Structural Insights into Arl1-Mediated Targeting of the Arf-GEF BIG1 to the trans-Golgi.Cell reports · 2016Article
- The Sec7 N-terminal regulatory domains facilitate membrane-proximal activation of the Arf1 GTPase.eLife · 2016Article
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Authors and funding
11 authors at 4 institutions in 1 country.
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Abstract
Members of the large Sec7 domain-containing Arf guanine nucleotide exchange factor (GEF) family have been shown to dimerize through their NH2-terminal dimerization and cyclophilin binding (DCB) and homology upstream of Sec7 (HUS) domains. However, the importance of dimerization in GEF localization and function has not been assessed. We generated a GBF1 mutant (91/130) in which two residues required for oligomerization (K91 and E130 within the DCB domain) were replaced with A and assessed the effects of these mutations on GBF1 localization and cellular functions. We show that 91/130 is compromised in oligomerization but that it targets to the Golgi in a manner indistinguishable from wild-type GBF1 and that it rapidly exchanges between the cytosolic and membrane-bound pools. The 91/130 mutant appears active as it integrates within the functional network at the Golgi, supports Arf activation and COPI recruitment, and sustains Golgi homeostasis and cargo secretion when provided as a sole copy of functional GBF1 in cells. In addition, like wild-type GBF1, the 91/130 mutant supports poliovirus RNA replication, a process requiring GBF1 but believed to be independent of GBF1 catalytic activity. However, oligomerization appears to stabilize GBF1 in cells, and the 91/130 mutant is degraded faster than the wild-type GBF1. Our data support a model in which oligomerization is not a key regulator of GBF1 activity but impacts its function by regulating the cellular levels of GBF1.
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