Loss of Pten, a tumor suppressor, causes the strong inhibition of autophagy without affecting LC3 lipidation
1Pten (phosphatase and tensin homolog deleted on chromosome ten), a tumor suppressor, is a phosphatase with a variety of substrate specificities. Its function as a negative regulator of the class I phosphatidyl-inositol 3-kinase/Akt pathway antagonizes insulin-dependent cell signaling. The targeted...
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Published in | Autophagy Vol. 4; no. 5; pp. 692 - 700 |
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Main Authors | , , , , , , , , , |
Format | Journal Article |
Language | English |
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United States
Taylor & Francis
01.07.2008
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Abstract | 1Pten (phosphatase and tensin homolog deleted on chromosome ten), a tumor suppressor, is a phosphatase with a variety of substrate specificities. Its function as a negative regulator of the class I phosphatidyl-inositol 3-kinase/Akt pathway antagonizes insulin-dependent cell signaling. The targeted deletion of Pten in mouse liver leads to insulin hypersensitivity and the upregulation of the phosphatidyl-inositol 3-kinase/Akt signaling pathway. In this study, we investigated the effects of Pten deficiency on autophagy, a major cellular degradative system responsible for the turnover of cell constituents. The autophagic degradation of [14C]-leucine-labeled proteins of hepatocytes isolated from Pten-deficient livers was strongly inhibited, compared with that of control hepatocytes. However, no significant difference was found in the levels of the Atg12-Atg5 conjugate and LC3-II, the lipidated form of LC3, an intrinsic autophagosomal membrane marker, between control and Pten-deficient livers. Electron microsopic analyses showed that numerous autophagic vacuoles (autophagosomes plus autolysosomes) were present in the livers of control mice that had been starved for 48 hours, whereas they were markedly reduced in Pten-deficient livers under the same conditions. In vivo administration of leupeptin to control livers caused the inhibition of autophagic proteolysis, resulting in the accumulation of autolysosomes. These autolysosomes could be separated as a denser autolysosomal fraction from other cell membranes by Percoll density gradient centrifugation. In leupeptin-administered mutant livers, however, the accumulation of denser autolysosomes was reduced substantially. Collectively, we conclude that enhanced insulin signaling in Pten deficiency suppresses autophagy at the formation and maturation steps of autophagosomes, without inhibiting ATG conjugation reactions. |
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AbstractList | (1)Pten (phosphatase and tensin homolog deleted on chromosome ten), a tumor suppressor, is a phosphatase with a variety of substrate specificities. Its function as a negative regulator of the class I phosphatidyl-inositol 3-kinase/Akt pathway antagonizes insulin-dependent cell signaling. The targeted deletion of Pten in mouse liver leads to insulin hypersensitivity and the upregulation of the phosphatidyl-inositol 3-kinase/Akt signaling pathway. In this study, we investigated the effects of Pten deficiency on autophagy, a major cellular degradative system responsible for the turnover of cell constituents. The autophagic degradation of [(14)C-leucine-labeled proteins of hepatocytes isolated from Pten-deficient livers was strongly inhibited, compared with that of control hepatocytes. However, no significant difference was found in the levels of the Atg12-Atg5 conjugate and LC3-II, the lipidated form of LC3, an intrinsic autophagosomal membrane marker, between control and Pten-deficient livers. Electron microscopic analyses showed that numerous autophagic vacuoles (autophagosomes plus autolysosomes) were present in the livers of control mice that had been starved for 48 hours, whereas they were markedly reduced in Pten-deficient livers under the same conditions. In vivo administration of leupeptin to control livers caused the inhibition of autophagic proteolysis, resulting in the accumulation of autolysosomes. These autolysosomes could be separated as a denser autolysosomal fraction from other cell membranes by Percoll density gradient centrifugation. In leupeptin-administered mutant livers, however, the accumulation of denser autolysosomes was reduced substantially. Collectively, we conclude that enhanced insulin signaling in Pten deficiency suppresses autophagy at the formation and maturation steps of autophagosomes, without inhibiting ATG conjugation reactions. 1Pten (phosphatase and tensin homolog deleted on chromosome ten), a tumor suppressor, is a phosphatase with a variety of substrate specificities. Its function as a negative regulator of the class I phosphatidyl-inositol 3-kinase/Akt pathway antagonizes insulin-dependent cell signaling. The targeted deletion of Pten in mouse liver leads to insulin hypersensitivity and the upregulation of the phosphatidyl-inositol 3-kinase/Akt signaling pathway. In this study, we investigated the effects of Pten deficiency on autophagy, a major cellular degradative system responsible for the turnover of cell constituents. The autophagic degradation of [14C]-leucine-labeled proteins of hepatocytes isolated from Pten-deficient livers was strongly inhibited, compared with that of control hepatocytes. However, no significant difference was found in the levels of the Atg12-Atg5 conjugate and LC3-II, the lipidated form of LC3, an intrinsic autophagosomal membrane marker, between control and Pten-deficient livers. Electron microsopic analyses showed that numerous autophagic vacuoles (autophagosomes plus autolysosomes) were present in the livers of control mice that had been starved for 48 hours, whereas they were markedly reduced in Pten-deficient livers under the same conditions. In vivo administration of leupeptin to control livers caused the inhibition of autophagic proteolysis, resulting in the accumulation of autolysosomes. These autolysosomes could be separated as a denser autolysosomal fraction from other cell membranes by Percoll density gradient centrifugation. In leupeptin-administered mutant livers, however, the accumulation of denser autolysosomes was reduced substantially. Collectively, we conclude that enhanced insulin signaling in Pten deficiency suppresses autophagy at the formation and maturation steps of autophagosomes, without inhibiting ATG conjugation reactions. |
Author | Watanabe, Sumio Sato, Wataru Horie, Yasuo Mak, Tak Wah Tanida, Isei Komatsu, Masaaki Kominami, Eiki Ueno, Takashi Yoshida, Mitsutaka Ohshima, Shigetoshi |
Author_xml | – sequence: 1 givenname: Takashi surname: Ueno fullname: Ueno, Takashi – sequence: 2 givenname: Wataru surname: Sato fullname: Sato, Wataru – sequence: 3 givenname: Yasuo surname: Horie fullname: Horie, Yasuo – sequence: 4 givenname: Masaaki surname: Komatsu fullname: Komatsu, Masaaki – sequence: 5 givenname: Isei surname: Tanida fullname: Tanida, Isei – sequence: 6 givenname: Mitsutaka surname: Yoshida fullname: Yoshida, Mitsutaka – sequence: 7 givenname: Shigetoshi surname: Ohshima fullname: Ohshima, Shigetoshi – sequence: 8 givenname: Tak Wah surname: Mak fullname: Mak, Tak Wah – sequence: 9 givenname: Sumio surname: Watanabe fullname: Watanabe, Sumio – sequence: 10 givenname: Eiki surname: Kominami fullname: Kominami, Eiki |
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Snippet | 1Pten (phosphatase and tensin homolog deleted on chromosome ten), a tumor suppressor, is a phosphatase with a variety of substrate specificities. Its function... (1)Pten (phosphatase and tensin homolog deleted on chromosome ten), a tumor suppressor, is a phosphatase with a variety of substrate specificities. Its... |
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SubjectTerms | Animals Apoptosis Regulatory Proteins - antagonists & inhibitors Apoptosis Regulatory Proteins - physiology Autophagy - genetics Autophagy - physiology Binding Biology Bioscience Calcium Cancer Cell Cells, Cultured Cycle Genes, Tumor Suppressor - physiology Hepatocytes - metabolism Hepatocytes - pathology Insulin - physiology Landes Lipid Metabolism - physiology Mice Mice, Inbred C57BL Mice, Transgenic Microtubule-Associated Proteins - metabolism Organogenesis Phagosomes - metabolism Proteins PTEN Phosphohydrolase - antagonists & inhibitors PTEN Phosphohydrolase - deficiency PTEN Phosphohydrolase - genetics Signal Transduction - genetics Starvation - metabolism |
Title | Loss of Pten, a tumor suppressor, causes the strong inhibition of autophagy without affecting LC3 lipidation |
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