A Snf1-related nutrient-responsive kinase antagonizes endocytosis in yeast

Autoři: Jessica M. Tumolo aff001;  Nathaniel L. Hepowit aff001;  Samika S. Joshi aff001;  Jason A. MacGurn aff001
Působiště autorů: Department of Cell and Developmental Biology, Vanderbilt University, Nashville, Tennessee, United States of America aff001
Vyšlo v časopise: A Snf1-related nutrient-responsive kinase antagonizes endocytosis in yeast. PLoS Genet 16(3): e1008677. doi:10.1371/journal.pgen.1008677
Kategorie: Research Article
doi: https://doi.org/10.1371/journal.pgen.1008677


Endocytosis is regulated in response to changing environmental conditions to adjust plasma membrane (PM) protein composition for optimal cell growth. Protein networks involved in cargo capture and sorting, membrane sculpting and deformation, and vesicle scission have been well-characterized, but less is known about the networks that sense extracellular cues and relay signals to trigger endocytosis of specific cargo. Hal4 and Hal5 are yeast Snf1-related kinases that were previously reported to regulate nutrient transporter stability by an unknown mechanism. Here we demonstrate that loss of Hal4 and Hal5 activates endocytosis of many different kinds of PM proteins, including Art1-mediated and Art1-independent endocytic events. Acute inhibition of Hal5 in the absence of Hal4 triggers rapid endocytosis, suggesting that Hal kinases function in a nutrient-sensing relay upstream of the endocytic response. Interestingly, Hal5 localizes to the PM, but shifts away from the cell surface in response to stimulation with specific nutrients. We propose that Hal5 functions as a nutrient-responsive regulator of PM protein stability, antagonizing endocytosis and promoting stability of endocytic cargos at the PM in nutrient-limiting conditions.

Klíčová slova:

Endocytosis – Membrane proteins – Phosphorylation – Protein transport – Sequence alignment – Statistical data – Vacuoles – Yeast


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