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 language | English (US) |
|---|---|
| Pages (from-to) | 977-992 |
| Number of pages | 16 |
| Journal | Journal of Cell Biology |
| Volume | 218 |
| Issue number | 3 |
| DOIs | |
| State | Published - Mar 1 2019 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Cell Biology
Cite this
Methionine triggers Ppz-mediated dephosphorylation of Art1 to promote cargo-specific endocytosis. / Lee, Sora; Ho, Hsuan Chung; Tumolo, Jessica M.; Hsu, Pi Chiang; MacGurn, Jason A.
In: Journal of Cell Biology, Vol. 218, No. 3, 01.03.2019, p. 977-992.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Methionine triggers Ppz-mediated dephosphorylation of Art1 to promote cargo-specific endocytosis
AU - Lee, Sora
AU - Ho, Hsuan Chung
AU - Tumolo, Jessica M.
AU - Hsu, Pi Chiang
AU - MacGurn, Jason A.
PY - 2019/3/1
Y1 - 2019/3/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=85062412625&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85062412625&partnerID=8YFLogxK
U2 - 10.1083/jcb.201712144
DO - 10.1083/jcb.201712144
M3 - Article
C2 - 30610170
AN - SCOPUS:85062412625
VL - 218
SP - 977
EP - 992
JO - Journal of Cell Biology
JF - Journal of Cell Biology
SN - 0021-9525
IS - 3
ER -