ArticleMolecular biology of the cell2015
Casein kinase 1 controls the activation threshold of an α-arrestin by multisite phosphorylation of the interdomain hinge.
Article in Molecular biology of the cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 23 citations in OpenAlex.
- Casein kinase 1α mediates eryptosis: a review.Apoptosis : an international journal on programmed cell death · 2023Review
- Conserved and Divergent Features of pH Sensing in Major Fungal Pathogens.Current clinical microbiology reports · 2023Review
- Article
- α-Arrestins and Their Functions: From Yeast to Human Health.International journal of molecular sciences · 2022Review
- TORC1 Signaling Controls the Stability and Function of α-Arrestins Aly1 and Aly2.Biomolecules · 2022Article
- A conserved ATG2 binding site in WIPI4 and yeast Hsv2 is disrupted by mutations causing β-propeller protein-associated neurodegeneration.Human molecular genetics · 2021Article
- Yck1 casein kinase I regulates the activity and phosphorylation of Pah1 phosphatidate phosphatase fromThe Journal of biological chemistry · 2019Article
- Evolutionary engineering and molecular characterization of a caffeine-resistant Saccharomyces cerevisiae strain.World journal of microbiology & biotechnology · 2019Article
- Yeast α-arrestin Art2 is the key regulator of ubiquitylation-dependent endocytosis of plasma membrane vitamin B1 transporters.PLoS biology · 2019Article
- AMPK-Mediated Regulation of Alpha-Arrestins and Protein Trafficking.International journal of molecular sciences · 2019Review
- Compensatory Internalization of Pma1 in V-ATPase Mutants inGenetics · 2018Article
- Involvement of the exomer complex in the polarized transport of Ena1 required forMolecular biology of the cell · 2017Article
- Improved α-Amylase Production by Dephosphorylation Mutation of CreD, an Arrestin-Like Protein Required for Glucose-Induced Endocytosis of Maltose Permease and Carbon Catabolite Derepression in Aspergillus oryzae.Applied and environmental microbiology · 2017Article
- Deubiquitinating enzymes Ubp2 and Ubp15 regulate endocytosis by limiting ubiquitination and degradation of ARTs.Molecular biology of the cell · 2017Article
- Mutational analysis of the Aspergillus ambient pH receptor PalH underscores its potential as a target for antifungal compounds.Molecular microbiology · 2016Article
- Article
- 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
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
α-Arrestins play a key role as trafficking adaptors in both yeast and mammals. The yeast Rim8/Art9 α-arrestin mediates the recruitment of endosomal sorting complex required for transport (ESCRT) to the seven-transmembrane protein Rim21 in the ambient pH signaling RIM pathway. ESCRT is believed to function as a signaling platform that enables the proteolytic activation of the Rim101 transcription factor upon external alkalization. Here we provide evidence that the pH signal promotes the stable association of Rim8 with Rim21 at the plasma membrane. We show that Rim8 is phosphorylated in a pH-independent but Rim21-dependent manner by the plasma membrane-associated casein kinase 1 (CK1). We further show that this process involves a cascade of phosphorylation events within the hinge region connecting the arrestin domains. Strikingly, loss of casein kinase 1 activity causes constitutive activation of the RIM pathway, and, accordingly, pH signaling is activated in a phosphodeficient Rim8 mutant and impaired in the corresponding phosphomimetic mutant. Our results indicate that Rim8 phosphorylation prevents its accumulation at the plasma membrane at acidic pH and thereby inhibits RIM signaling. These findings support a model in which CK1-mediated phosphorylation of Rim8 contributes to setting a signaling threshold required to inhibit the RIM pathway at acidic pH.
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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.