Methionine triggers Ppz-mediated dephosphorylation of Art1 to promote cargo-specific endocytosis

Sora Lee, Hsuan Chung Ho, Jessica M. Tumolo, Pi Chiang Hsu, Jason A. MacGurn

Research output: Contribution to journalArticle

3 Scopus citations

Abstract

Regulation of plasma membrane (PM) protein abundance by selective endocytosis is critical for cellular adaptation to stress or changing nutrient availability. One example involves rapid endocytic turnover of Mup1, a yeast methionine transporter, in response to increased methionine availability. Here, we report that methionine triggers rapid translocation of the ubiquitin ligase adaptor Art1 to the PM and dephosphorylation of Art1 at specific threonine residues. This methionine-induced dephosphorylation of Art1 is mediated by Ppz phosphatases, and analysis of phosphomimetic and phosphorylation-defective variants of Art1 indicates that these events toggle Art1 recognition of Mup1 at the PM. Importantly, we find that Ppz phosphatases are dispensable for Art1 PM translocation, but are required for Art1 interaction with Mup1. Based on our findings, we propose that methionine influx triggers Art1 translocation to the PM, followed by Ppz-mediated dephosphorylation which promotes cargo recognition at the PM.

Original languageEnglish (US)
Pages (from-to)977-992
Number of pages16
JournalJournal of Cell Biology
Volume218
Issue number3
DOIs
Publication statusPublished - Mar 1 2019
Externally publishedYes

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ASJC Scopus subject areas

  • Cell Biology

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