ArticleEukaryotic cell2012
The β-arrestin-like protein Rim8 is hyperphosphorylated and complexes with Rim21 and Rim101 to promote adaptation to neutral-alkaline pH.
Article in Eukaryotic cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
What it found
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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
26 citing papers in PubMed, 34 citations in OpenAlex.
- Morphotype-specific susceptibility toMicrobiology spectrum · 2026Article
- Proteomic characterization of clinical Candida glabrata isolates with varying degrees of virulence and resistance to fluconazole.PloS one · 2025Article
- In Vitro Acid Resistance of PathogenicGastro hep advances · 2025Article
- The Arrestin-like Protein palF Contributes to Growth, Sporulation, Spore Germination, Osmolarity, and Pathogenicity ofJournal of fungi (Basel, Switzerland) · 2024Article
- Transcriptional expression ofMicrobiology spectrum · 2024Article
- Developing novel antifungals: lessons from G protein-coupled receptors.Trends in pharmacological sciences · 2023Review
- Conserved and Divergent Features of pH Sensing in Major Fungal Pathogens.Current clinical microbiology reports · 2023Review
- Article
- Candida albicans Morphogenesis Programs Control the Balance between Gut Commensalism and Invasive Infection.Cell host & microbe · 2019Article
- AMPK-Mediated Regulation of Alpha-Arrestins and Protein Trafficking.International journal of molecular sciences · 2019Review
- The Rim Pathway Mediates Antifungal Tolerance in Candida albicans through Newly Identified Rim101 Transcriptional Targets, Including Hsp90 and Ipt1.Antimicrobial agents and chemotherapy · 2018Article
- Compensatory Internalization of Pma1 in V-ATPase Mutants inGenetics · 2018Article
- Candida albicans cell-type switching and functional plasticity in the mammalian host.Nature reviews. Microbiology · 2017Review
- Morphology Changes in Human Fungal Pathogens upon Interaction with the Host.Journal of fungi (Basel, Switzerland) · 2017Article
- Molecular Components of the Neurospora crassa pH Signaling Pathway and Their Regulation by pH and the PAC-3 Transcription Factor.PloS one · 2016Article
- The C-terminal Cytosolic Region of Rim21 Senses Alterations in Plasma Membrane Lipid Composition: INSIGHTS INTO SENSING MECHANISMS FOR PLASMA MEMBRANE LIPID ASYMMETRY.The Journal of biological chemistry · 2015Article
- Refining the pH response in Aspergillus nidulans: a modulatory triad involving PacX, a novel zinc binuclear cluster protein.Molecular microbiology · 2015Article
- Casein kinase 1 controls the activation threshold of an α-arrestin by multisite phosphorylation of the interdomain hinge.Molecular biology of the cell · 2015Article
- Loss of vacuolar H+-ATPase activity in organelles signals ubiquitination and endocytosis of the yeast plasma membrane proton pump Pma1p.The Journal of biological chemistry · 2014Article
- Fungal morphogenesis.Cold Spring Harbor perspectives in medicine · 2014Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
β-Arrestin proteins are critical for G-protein-coupled receptor desensitization and turnover. However, β-arrestins have recently been shown to play direct roles in nonheterotrimeric G-protein signal transduction. The Candida albicans β-arrestin-like protein Rim8 is required for activation of the Rim101 pH-sensing pathway and for pathogenesis. We have found that C. albicans Rim8 is posttranslationally modified by phosphorylation and specific phosphorylation states are associated with activation of the pH-sensing pathway. Rim8 associated with both the receptor Rim21 and the transcription factor Rim101, suggesting that Rim8 bridges the signaling and activation steps of the pathway. Finally, upon activation of the Rim101 transcription factor, C. albicans Rim8 was transcriptionally repressed and Rim8 protein levels were rapidly reduced. Our studies suggest that Rim8 is taken up into multivesicular bodies and degraded within the vacuole. In total, our results reveal a novel mechanism for tightly regulating the activity of a signal transduction pathway. Although the role of β-arrestin proteins in mammalian signal transduction pathways has been demonstrated, relatively little is known about how β-arrestins contribute to signal transduction. Our analyses provide some insights into potential roles.
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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.