Tor Directly Controls the Atg1 Kinase Complex To Regulate Autophagy
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| Veröffentlicht in: | Molecular and Cellular Biology Jg. 30; H. 4; S. 1049 - 1058 |
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| Sprache: | Englisch |
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American Society for Microbiology
01.02.2010
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Autophagy is a bulk proteolytic process that is indispensable for cell survival during starvation. Autophagy is induced by nutrient deprivation via inactivation of the rapamycin-sensitive Tor complex1 (TORC1), a protein kinase complex regulating cell growth in response to nutrient conditions. However, the mechanism by which TORC1 controls autophagy and the direct target of TORC1 activity remain unclear. Atg13 is an essential regulatory component of autophagy upstream of the Atg1 kinase complex, and here we show that yeast TORC1 directly phosphorylates Atg13 at multiple Ser residues. Additionally, expression of an unphosphorylatable Atg13 mutant bypasses the TORC1 pathway to induce autophagy through activation of Atg1 in cells growing under nutrient-rich conditions. Our findings suggest that the direct control of the Atg1 complex by TORC1 induces autophagy. Autophagy is a bulk proteolytic process that is indispensable for cell survival during starvation. Autophagy is induced by nutrient deprivation via inactivation of the rapamycin-sensitive Tor complex1 (TORC1), a protein kinase complex regulating cell growth in response to nutrient conditions. However, the mechanism by which TORC1 controls autophagy and the direct target of TORC1 activity remain unclear. Atg13 is an essential regulatory component of autophagy upstream of the Atg1 kinase complex, and here we show that yeast TORC1 directly phosphorylates Atg13 at multiple Ser residues. Additionally, expression of an unphosphorylatable Atg13 mutant bypasses the TORC1 pathway to induce autophagy through activation of Atg1 in cells growing under nutrient-rich conditions. Our findings suggest that the direct control of the Atg1 complex by TORC1 induces autophagy.Autophagy is a bulk proteolytic process that is indispensable for cell survival during starvation. Autophagy is induced by nutrient deprivation via inactivation of the rapamycin-sensitive Tor complex1 (TORC1), a protein kinase complex regulating cell growth in response to nutrient conditions. However, the mechanism by which TORC1 controls autophagy and the direct target of TORC1 activity remain unclear. Atg13 is an essential regulatory component of autophagy upstream of the Atg1 kinase complex, and here we show that yeast TORC1 directly phosphorylates Atg13 at multiple Ser residues. Additionally, expression of an unphosphorylatable Atg13 mutant bypasses the TORC1 pathway to induce autophagy through activation of Atg1 in cells growing under nutrient-rich conditions. Our findings suggest that the direct control of the Atg1 complex by TORC1 induces autophagy. |
| Author | Chika Kondo Noriko Oshiro Tomoko Kawamata Ken-ichi Yoshino Kazuyoshi Yonezawa Yoshinori Ohsumi Yoshiaki Kamada |
| AuthorAffiliation | Division of Molecular Cell Biology, National Institute for Basic Biology, Okazaki 444-8585, Japan, 1 Biosignal Research Center, Kobe University, Kobe 657-8501, Japan 2 |
| AuthorAffiliation_xml | – name: Division of Molecular Cell Biology, National Institute for Basic Biology, Okazaki 444-8585, Japan, 1 Biosignal Research Center, Kobe University, Kobe 657-8501, Japan 2 |
| Author_xml | – sequence: 1 givenname: Yoshiaki surname: Kamada fullname: Kamada, Yoshiaki email: yoshikam@nibb.ac.jp, yohsumi@iri.titech.ac.jp organization: Division of Molecular Cell Biology, National Institute for Basic Biology – sequence: 2 givenname: Ken-ichi surname: Yoshino fullname: Yoshino, Ken-ichi organization: Biosignal Research Center, Kobe University – sequence: 3 givenname: Chika surname: Kondo fullname: Kondo, Chika organization: Division of Molecular Cell Biology, National Institute for Basic Biology – sequence: 4 givenname: Tomoko surname: Kawamata fullname: Kawamata, Tomoko organization: Division of Molecular Cell Biology, National Institute for Basic Biology – sequence: 5 givenname: Noriko surname: Oshiro fullname: Oshiro, Noriko organization: Biosignal Research Center, Kobe University – sequence: 6 givenname: Kazuyoshi surname: Yonezawa fullname: Yonezawa, Kazuyoshi organization: Biosignal Research Center, Kobe University – sequence: 7 givenname: Yoshinori surname: Ohsumi fullname: Ohsumi, Yoshinori email: yoshikam@nibb.ac.jp, yohsumi@iri.titech.ac.jp organization: Division of Molecular Cell Biology, National Institute for Basic Biology |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/19995911$$D View this record in MEDLINE/PubMed |
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| SubjectTerms | Amino Acid Sequence Autophagy Autophagy-Related Proteins Microscopy, Electron Molecular Sequence Data Phosphorylation Protein Binding Protein Kinases - chemistry Protein Kinases - genetics Protein Kinases - metabolism Protein-Serine-Threonine Kinases - genetics Protein-Serine-Threonine Kinases - metabolism Saccharomyces cerevisiae - cytology Saccharomyces cerevisiae - enzymology Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism |
| Title | Tor Directly Controls the Atg1 Kinase Complex To Regulate Autophagy |
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