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Τύπος: Άρθρο σε επιστημονικό περιοδικό
Τίτλος: The Bul1/2 alpha-arrestins promote ubiquitylation and endocytosis of the Can1 permease upon cycloheximide-induced TORC1-hyperactivation
Συγγραφέας: [EL] Μεγαριώτη, Αμαλία[EN] Megarioti, Amaliasemantics logo
[FR] Primo, Ceciliasemantics logo
[EL] Καπετανάκης, Γεώργιος[EN] Kapetanakis, Georgesemantics logo
[EL] Αθανασόπουλος, Αλέξανδρος[EN] Athanasopoulos, Alexandrossemantics logo
[EL] Σοφιανοπούλου, Βασιλική[EN] Sophianopoulou, Vassilikisemantics logo
[FR] André, Brunosemantics logo
[EL] Γουρνάς, Χρήστος[EN] Gournas, Christossemantics logo
Ημερομηνία: 22/09/2021
Περίληψη: Selective endocytosis followed by degradation is a major mechanism for downregulating plasma membrane transporters in response to specific environmental cues. In Saccharomyces cerevisiae, this endocytosis is promoted by ubiquitylation catalyzed by the Rsp5 ubiquitin-ligase, targeted to transporters via adaptors of the alpha-arrestin family. However, the molecular mechanisms of this targeting and their control according to conditions remain incompletely understood. In this work, we dissect the molecular mechanisms eliciting the endocytosis of Can1, the arginine permease, in response to cycloheximide-induced TORC1 hyperactivation. We show that cycloheximide promotes Rsp5-dependent Can1 ubiquitylation and endocytosis in a manner dependent on the Bul1/2 alpha- arrestins. Also crucial for this downregulation is a short acidic patch sequence in the N-terminus of Can1 likely acting as a binding site for Bul1/2. The previously reported inhibition by cycloheximide of transporter recycling, from the trans-Golgi network to the plasma membrane, seems to additionally contribute to efficient Can1 downregulation. Our results also indicate that, contrary to the previously described substrate-transport elicited Can1 endocytosis mediated by the Art1 alpha-arrestin, Bul1/2- mediated Can1 ubiquitylation occurs independently of the conformation of the transporter. This study provides further insights into how distinct alpha-arrestins control the ubiquitin-dependent downregulation of a specific amino acid transporter under different conditions.
Γλώσσα: Αγγλικά
Σελίδες: 18
DOI: 10.3390/ijms221910208
EISSN: 1422-0067
Θεματική κατηγορία: [EL] Βιολογία[EN] Biologysemantics logo
Λέξεις-κλειδιά: ubiquitinα-arrestinendocytosistransporterarginineTarget of Rapamycin Complex 1Npr1acidic patchNedd4
Κάτοχος πνευματικών δικαιωμάτων: © 2021 by the authors. Licensee MDPI, Basel, Switzerland.
Όροι και προϋποθέσεις δικαιωμάτων: This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https:// creativecommons.org/licenses/by/ 4.0/).
Σχετίζεται με: The organization of the fungal plasma membrane in the quiescent state
Ηλεκτρονική διεύθυνση του τεκμηρίου στον εκδότη: https://www.mdpi.com/1422-0067/22/19/10208
Ηλεκτρονική διεύθυνση περιοδικού: https://www.mdpi.com/journal/ijms
Τίτλος πηγής δημοσίευσης: International Journal of Molecular Sciences
Τεύχος: 19
Τόμος: 22
Σελίδες τεκμηρίου (στην πηγή): Article no 10208
Σημειώσεις: This research is co-financed by Greece and the European Union (European Social FundESF) through the Operational Programme «Human Resources Development, Education and Lifelong Learning 2014–2020» in the context of the project “Study of the role of eisosomal proteins in the quiescent state of fungal cells” (MIS 5047827)
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