Starvation-induced degradation of yeast hexose transporter Hxt7p is dependent on endocytosis, autophagy and the terminal sequences of the permease

FEBS Letters
S Krampe, E Boles

Abstract

The yeast high-affinity glucose transporters Hxt6p and Hxt7p are rapidly degraded during nitrogen starvation in the presence of high concentrations of fermentable carbon sources. Our results suggest that degradation is mainly due to the stimulation of general protein turnover and not caused by a mechanism specifically triggered by glucose. Analysis of Hxt6p/7p stability and cellular distribution in end4, aut2 and apg1 mutants indicates that Hxt7p is internalized by endocytosis, and autophagy is involved in the final delivery of Hxt7p to the vacuole for proteolytic degradation. Internalization and degradation of Hxt7p were blocked after truncation of its N-terminal hydrophilic domain. Nevertheless, this fully functional and stabilized hexose transporter could not maintain fermentation capacity of the yeast cells under starvation conditions, indicating a regulatory constraint on glucose uptake.

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Citations

Mar 5, 2013·Current Genetics·J Horák
Mar 23, 2005·FEMS Yeast Research·Sergio RossellHans V Westerhoff
Jun 1, 2005·FEMS Yeast Research·Jennifer M GardnerVladimir Jiranek
Jun 19, 2013·Current Opinion in Cell Biology·Markus Babst, Greg Odorizzi
Mar 30, 2005·The FEBS Journal·Karin A ReijengaHans V Westerhoff
Aug 25, 2006·Biology of the Cell·Denise van SuylekomJohannes Boonstra
Nov 29, 2011·Traffic·Charles B JonesMarkus Babst
Jul 24, 2015·Applied Microbiology and Biotechnology·Catherine TesnièreBruno Blondin
Sep 22, 2010·Molecular Plant-microbe Interactions : MPMI·Hun Kim, Charles P Woloshuk
Jul 19, 2002·Yeast
Oct 18, 2019·Traffic·Sadia RahmaniCostin N Antonescu
Mar 20, 2019·Molecular and Cellular Biology·Marco JochemJohn Hanna
Apr 27, 2021·Computational and Structural Biotechnology Journal·Cláudia Barata-AntunesSandra Paiva

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