ArticleMolecular biology of the cell2003
A novel Golgi membrane protein is a partner of the ARF exchange factors Gea1p and Gea2p.
Article in Molecular biology of the cell, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 55 citations in OpenAlex.
- Article
- Viral protein engagement of GBF1 induces host cell vulnerability through synthetic lethality.The Journal of cell biology · 2022Article
- Stability Analysis of a Signaling Circuit with Dual Species of GTPase Switches.Bulletin of mathematical biology · 2021Article
- Viral protein engagement of GBF1 induces host cell vulnerability through synthetic lethality.bioRxiv : the preprint server for biology · 2020Article
- BioID Performed on Golgi Enriched Fractions Identify C10orf76 as a GBF1 Binding Protein Essential for Golgi Maintenance and Secretion.Molecular & cellular proteomics : MCP · 2019Article
- Regulation of Arf activation occurs via distinct mechanisms at early and late Golgi compartments.Molecular biology of the cell · 2017Article
- Genome-wide siRNA screen identifies UNC50 as a regulator of Shiga toxin 2 trafficking.The Journal of cell biology · 2017Article
- High phosphatidylinositol 4-phosphate (PI4P)-dependent ATPase activity for the Drs2p-Cdc50p flippase after removal of its N- and C-terminal extensions.The Journal of biological chemistry · 2017Article
- UNC50 prompts G1/S transition and proliferation in HCC by regulation of epidermal growth factor receptor trafficking.PloS one · 2015Article
- GBF/Gea mutant with a single substitution sustains fungal growth in the absence of BIG/Sec7.FEBS letters · 2014Article
- Regulating the large Sec7 ARF guanine nucleotide exchange factors: the when, where and how of activation.Cellular and molecular life sciences : CMLS · 2014Review
- Rewiring of cellular membrane homeostasis by picornaviruses.Journal of virology · 2014Review
- Virus entry. Lassa virus entry requires a trigger-induced receptor switch.Science (New York, N.Y.) · 2014Article
- Molecular mechanisms of Sar/Arf GTPases in vesicular trafficking in yeast and plants.Frontiers in plant science · 2014Review
- The Sec7 Arf-GEF is recruited to the trans-Golgi network by positive feedback.Developmental cell · 2012Article
- Trs65p, a subunit of the Ypt1p GEF TRAPPII, interacts with the Arf1p exchange factor Gea2p to facilitate COPI-mediated vesicle traffic.Molecular biology of the cell · 2011Article
- Article
- Large Arf1 guanine nucleotide exchange factors: evolution, domain structure, and roles in membrane trafficking and human disease.Molecular genetics and genomics : MGG · 2009Review
- GEF1 is a ciliary Sec7 GEF of Tetrahymena thermophila.Cell motility and the cytoskeleton · 2009Article
- GNOM-mediated vesicular trafficking plays an essential role in hydrotropism of Arabidopsis roots.Plant physiology · 2009Article
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Authors and funding
6 authors at 2 institutions in 1 country.
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Abstract
The Sec7 domain guanine nucleotide exchange factors (GEFs) for the GTPase ARF are highly conserved regulators of membrane dynamics and protein trafficking. The interactions of large ARF GEFs with cellular membranes for localization and/or activation are likely to participate in regulated recruitment of ARF and effectors. However, these interactions remain largely unknown. Here we characterize Gmh1p, the first Golgi transmembrane-domain partner of any of the high-molecular-weight ARF-GEFs. Gmh1p is an evolutionarily conserved protein. We demonstrate molecular interaction between the yeast Gmh1p and the large ARF-GEFs Gea1p and Gea2p. This interaction involves a domain of Gea1p and Gea2p that is conserved in the eukaryotic orthologues of the Gea proteins. A single mutation in a conserved amino acid residue of this domain is sufficient to abrogate the interaction, whereas the overexpression of Gmh1p can compensate in vivo defects caused by mutations in this domain. We show that Gmh1p is an integral membrane protein that localizes to the early Golgi in yeast and in human HeLa cells and cycles through the ER. Hence, we propose that Gmh1p acts as a positive Golgi-membrane partner for Gea function. These results are of general interest given the evolutionary conservation of both ARF-GEFs and the Gmh proteins.
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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 OpenQuestion graph.