RapamycinFungusV1, Main, Exploration, bibRecord, 000A52

Orchestrated Action of PP2A Antagonizes Atg13 Phosphorylation and Promotes Autophagy after the Inactivation of TORC1.

Identifieur interne : 000A52 ( Main/Exploration ); précédent : 000A51; suivant : 000A53

Orchestrated Action of PP2A Antagonizes Atg13 Phosphorylation and Promotes Autophagy after the Inactivation of TORC1.

Auteurs : Akter Mst Yeasmin [Japon] ; Talukdar Muhammad Waliullah [Japon] ; Akihiro Kondo [Japon] ; Atsuki Kaneko [Japon] ; Naoki Koike [Japon] ; Takashi Ushimaru [Japon]

Source :

PloS one [ 1932-6203 ] ; 2016.

RBID : pubmed:27973551

Descripteurs français

English descriptors

KwdEn :
- Adaptor Proteins, Signal Transducing (metabolism), Autophagosomes (MeSH), Autophagy (MeSH), Autophagy-Related Proteins (metabolism), Cell Cycle Proteins (metabolism), Cytoplasm (metabolism), Green Fluorescent Proteins (metabolism), Phosphorylation (MeSH), Protein Kinases (metabolism), Protein Phosphatase 2 (metabolism), Saccharomyces cerevisiae (metabolism), Saccharomyces cerevisiae Proteins (metabolism), Sirolimus (chemistry), Transcription Factors (metabolism).
MESH :
- chemical , chemistry : Sirolimus.
- chemical , metabolism : Adaptor Proteins, Signal Transducing, Autophagy-Related Proteins, Cell Cycle Proteins, Green Fluorescent Proteins, Protein Kinases, Protein Phosphatase 2, Saccharomyces cerevisiae Proteins, Transcription Factors.
- metabolism : Cytoplasm, Saccharomyces cerevisiae.
- Autophagosomes, Autophagy, Phosphorylation.

Abstract

Target of rapamycin complex 1 (TORC1) phosphorylates autophagy-related Atg13 and represses autophagy under nutrient-rich conditions. However, when TORC1 becomes inactive upon nutrient depletion or treatment with the TORC1 inhibitor rapamycin, Atg13 dephosphorylation occurs rapidly, and autophagy is induced. At present, the phosphatases involved in Atg13 dephosphorylation remain unknown. Here, we show that two protein phosphatase 2A (PP2A) phosphatases, PP2A-Cdc55 and PP2A-Rts1, which are activated by inactivation of TORC1, are required for sufficient Atg13 dephosphorylation and autophagy induction after TORC1 inactivation in budding yeast. After rapamycin treatment, dephosphorylation of Atg13, activation of Atg1 kinase, pre-autophagosomal structure (PAS) formation and autophagy induction are all impaired in PP2A-deleted cells. Conversely, overexpression of non-phosphorylatable Atg13 suppressed defects in autophagy in PP2A mutant. This study revealed that the orchestrated action of PP2A antagonizes Atg13 phosphorylation and promotes autophagy after the inactivation of TORC1.

DOI: 10.1371/journal.pone.0166636
PubMed: 27973551
PubMed Central: PMC5156417

Affiliations:

Japon

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 000918
to stream Main, to step Curation: 000918

Le document en format XML

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<term>Autophagy-Related Proteins (metabolism)</term>
<term>Cell Cycle Proteins (metabolism)</term>
<term>Cytoplasm (metabolism)</term>
<term>Green Fluorescent Proteins (metabolism)</term>
<term>Phosphorylation (MeSH)</term>
<term>Protein Kinases (metabolism)</term>
<term>Protein Phosphatase 2 (metabolism)</term>
<term>Saccharomyces cerevisiae (metabolism)</term>
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<term>Autophagosomes (MeSH)</term>
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<term>Facteurs de transcription (métabolisme)</term>
<term>Phosphorylation (MeSH)</term>
<term>Protein Phosphatase 2 (métabolisme)</term>
<term>Protein kinases (métabolisme)</term>
<term>Protéines adaptatrices de la transduction du signal (métabolisme)</term>
<term>Protéines associées à l'autophagie (métabolisme)</term>
<term>Protéines de Saccharomyces cerevisiae (métabolisme)</term>
<term>Protéines du cycle cellulaire (métabolisme)</term>
<term>Protéines à fluorescence verte (métabolisme)</term>
<term>Saccharomyces cerevisiae (métabolisme)</term>
<term>Sirolimus (composition chimique)</term>
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<term>Protéines adaptatrices de la transduction du signal</term>
<term>Protéines associées à l'autophagie</term>
<term>Protéines de Saccharomyces cerevisiae</term>
<term>Protéines du cycle cellulaire</term>
<term>Protéines à fluorescence verte</term>
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<front><div type="abstract" xml:lang="en">Target of rapamycin complex 1 (TORC1) phosphorylates autophagy-related Atg13 and represses autophagy under nutrient-rich conditions. However, when TORC1 becomes inactive upon nutrient depletion or treatment with the TORC1 inhibitor rapamycin, Atg13 dephosphorylation occurs rapidly, and autophagy is induced. At present, the phosphatases involved in Atg13 dephosphorylation remain unknown. Here, we show that two protein phosphatase 2A (PP2A) phosphatases, PP2A-Cdc55 and PP2A-Rts1, which are activated by inactivation of TORC1, are required for sufficient Atg13 dephosphorylation and autophagy induction after TORC1 inactivation in budding yeast. After rapamycin treatment, dephosphorylation of Atg13, activation of Atg1 kinase, pre-autophagosomal structure (PAS) formation and autophagy induction are all impaired in PP2A-deleted cells. Conversely, overexpression of non-phosphorylatable Atg13 suppressed defects in autophagy in PP2A mutant. This study revealed that the orchestrated action of PP2A antagonizes Atg13 phosphorylation and promotes autophagy after the inactivation of TORC1.</div>
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<Abstract><AbstractText>Target of rapamycin complex 1 (TORC1) phosphorylates autophagy-related Atg13 and represses autophagy under nutrient-rich conditions. However, when TORC1 becomes inactive upon nutrient depletion or treatment with the TORC1 inhibitor rapamycin, Atg13 dephosphorylation occurs rapidly, and autophagy is induced. At present, the phosphatases involved in Atg13 dephosphorylation remain unknown. Here, we show that two protein phosphatase 2A (PP2A) phosphatases, PP2A-Cdc55 and PP2A-Rts1, which are activated by inactivation of TORC1, are required for sufficient Atg13 dephosphorylation and autophagy induction after TORC1 inactivation in budding yeast. After rapamycin treatment, dephosphorylation of Atg13, activation of Atg1 kinase, pre-autophagosomal structure (PAS) formation and autophagy induction are all impaired in PP2A-deleted cells. Conversely, overexpression of non-phosphorylatable Atg13 suppressed defects in autophagy in PP2A mutant. This study revealed that the orchestrated action of PP2A antagonizes Atg13 phosphorylation and promotes autophagy after the inactivation of TORC1.</AbstractText>
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<Initials>AM</Initials>
<AffiliationInfo><Affiliation>Graduate School of Science and Technology, Shizuoka University, Suruga-ku, Shizuoka, Japan.</Affiliation>
</AffiliationInfo>
</Author>
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<ForeName>Talukdar Muhammad</ForeName>
<Initials>TM</Initials>
<AffiliationInfo><Affiliation>Graduate School of Science and Technology, Shizuoka University, Suruga-ku, Shizuoka, Japan.</Affiliation>
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<ForeName>Atsuki</ForeName>
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<Initials>N</Initials>
<AffiliationInfo><Affiliation>Faculty of Science, Shizuoka University, Suruga-ku, Shizuoka, Japan.</Affiliation>
</AffiliationInfo>
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<ForeName>Takashi</ForeName>
<Initials>T</Initials>
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</AffiliationInfo>
<AffiliationInfo><Affiliation>Faculty of Science, Shizuoka University, Suruga-ku, Shizuoka, Japan.</Affiliation>
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<Month>12</Month>
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<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
</MeshHeadingList>
<CoiStatement>The authors have declared that no competing interests exist.</CoiStatement>
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<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2016</Year>
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Orchestrated Action of PP2A Antagonizes Atg13 Phosphorylation and Promotes Autophagy after the Inactivation of TORC1.

Orchestrated Action of PP2A Antagonizes Atg13 Phosphorylation and Promotes Autophagy after the Inactivation of TORC1.

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