ArticleMolecular biology of the cell2012
The phosphoinositide-associated protein Rush hour regulates endosomal trafficking in Drosophila.
Article in Molecular biology of the cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 16 citations in OpenAlex.
- Synthetic biology approaches to generate temperature-sensitive alleles for the Sterile Insect Technique.Insect science · 2026Review
- Alternative mechanisms of Notch activation by partitioning into distinct endosomal domains.The Journal of cell biology · 2024Article
- Deep orange gene editing triggers temperature-sensitive lethal phenotypes in Ceratitis capitata.BMC biotechnology · 2024Article
- The role of Phafin proteins in cell signaling pathways and diseases.Open life sciences · 2024Review
- Phafins Are More Than Phosphoinositide-Binding Proteins.International journal of molecular sciences · 2023Review
- The PH Domain and C-Terminal polyD Motif of Phafin2 Exhibit a Unique Concurrence in Animals.Membranes · 2022Article
- BackboneBiomolecular NMR assignments · 2022Article
- Quantitative analyses of EGFR localization and trafficking dynamics in the follicular epithelium.Development (Cambridge, England) · 2020Article
- Structural, thermodynamic, and phosphatidylinositol 3-phosphate binding properties of Phafin2.Protein science : a publication of the Protein Society · 2017Article
- A LAPF/phafin1-like protein regulates TORC1 and lysosomal membrane permeabilization in response to endoplasmic reticulum membrane stress.Molecular biology of the cell · 2015Article
- Polarization and myelination in myelinating glia.ISRN neurology · 2012Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Endocytosis regulates multiple cellular processes, including the protein composition of the plasma membrane, intercellular signaling, and cell polarity. We have identified the highly conserved protein Rush hour (Rush) and show that it participates in the regulation of endocytosis. Rush localizes to endosomes via direct binding of its FYVE (Fab1p, YOTB, Vac1p, EEA1) domain to phosphatidylinositol 3-phosphate. Rush also directly binds to Rab GDP dissociation inhibitor (Gdi), which is involved in the activation of Rab proteins. Homozygous rush mutant flies are viable but show genetic interactions with mutations in Gdi, Rab5, hrs, and carnation, the fly homologue of Vps33. Overexpression of Rush disrupts progression of endocytosed cargo and increases late endosome size. Lysosomal marker staining is decreased in Rush-overexpressing cells, pointing to a defect in the transition between late endosomes and lysosomes. Rush also causes formation of endosome clusters, possibly by affecting fusion of endosomes via an interaction with the class C Vps/homotypic fusion and vacuole protein-sorting (HOPS) complex. These results indicate that Rush controls trafficking from early to late endosomes and from late endosomes to lysosomes by modulating the activity of Rab proteins.
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