ArticleGenetics2003
A role for GEA1 and GEA2 in the organization of the actin cytoskeleton in Saccharomyces cerevisiae.
Article in Genetics, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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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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Who cites it
7 citing papers in PubMed.
- The Arf activator GBF1 localizes to plasma membrane sites involved in cell adhesion and motility.Cellular logistics · 2017Article
- Arf3p GTPase is a key regulator of Bud2p activation for invasive growth in Saccharomyces cerevisiae.Molecular biology of the cell · 2013Article
- Haploinsufficiency of the Sec7 guanine nucleotide exchange factor gea1 impairs septation in fission yeast.PloS one · 2013Article
- Triangle network motifs predict complexes by complementing high-error interactomes with structural information.BMC bioinformatics · 2009Article
- Yeast Arf3p modulates plasma membrane PtdIns(4,5)P2 levels to facilitate endocytosis.Traffic (Copenhagen, Denmark) · 2008Article
- Regulation of nicotinic receptor trafficking by the transmembrane Golgi protein UNC-50.The EMBO journal · 2007Article
- Identification of a guanine nucleotide exchange factor for Arf3, the yeast orthologue of mammalian Arf6.PloS one · 2007Article
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Profilin is an actin monomer-binding protein implicated in the polymerization of actin filaments. In the budding yeast Saccharomyces cerevisiae, the pfy1-111 rho2delta double mutant has severe growth and actin cytoskeletal defects. The GEA1 and GEA2 genes, which code for paralog guanosine exchange factors for Arf proteins, were identified as multicopy suppressors of the mutant phenotype. These two genes restored the polarized distribution of actin cortical patches and produced visible actin cables in both the pfy1-111 rho2delta and pfy1delta cells. Thus, overexpression of GEA1 or GEA2 bypassed the requirement for profilin in actin cable formation. In addition, gea1 gea2 double mutants showed defects in budding and in actin cytoskeleton organization, while overexpression of GEA1 or GEA2 led to the formation of supernumerary actin cable-like structures in a Bni1p/Bnr1p-dependent manner. The ADP-ribosylation factor Arf3p may be a target of Gea1p/Gea2p, since overexpression of ARF3 partially suppressed the profilin-deficient phenotype and a deletion of ARF3 exacerbated the phenotype of a pfy1-111 mutant. Gea1p, Gea2p, Arf1p, and Arf2p but not Arf3p are known to function in vesicular transport between the endoplasmic reticulum and the Golgi. In this work, we demonstrate a role for Gea1p, Gea2p, and Arf3p in the organization of the actin cytoskeleton.
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