Rapamycin activates mammalian microautophagy
Autophagy-lysosome proteolysis is classified into macroautophagy (MA), microautophagy (mA) and chaperone-mediated autophagy (CMA). In contrast to MA and CMA, mA have been mainly studied in yeast. In 2011, mammalian mA was identified as a pathway to deliver cytosolic proteins into multivesicular bodi...
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doaj-1259e534934d4baaa4deac5c42c6851b2020-11-25T02:46:51ZengElsevierJournal of Pharmacological Sciences1347-86132019-06-011402201204Rapamycin activates mammalian microautophagyMasahiro Sato0Takahiro Seki1Ayumu Konno2Hirokazu Hirai3Yuki Kurauchi4Akinori Hisatsune5Hiroshi Katsuki6Department of Chemico-Pharmacological Sciences, Graduate School of Pharmaceutical Sciences, Kumamoto University, Kumamoto, JapanDepartment of Chemico-Pharmacological Sciences, Graduate School of Pharmaceutical Sciences, Kumamoto University, Kumamoto, Japan; Corresponding author. Department of Chemico-Pharmacological Sciences, Graduate School of Pharmaceutical Sciences, Kumamoto University, 5-1 Oe-Honmachi, Chuo-ku, Kumamoto 862-0973, Japan. Fax: +81 96 371 4182.Department of Neurophysiology & Neural Repair, Gunma University Graduate School of Medicine, Maebashi, JapanDepartment of Neurophysiology & Neural Repair, Gunma University Graduate School of Medicine, Maebashi, JapanDepartment of Chemico-Pharmacological Sciences, Graduate School of Pharmaceutical Sciences, Kumamoto University, Kumamoto, JapanDepartment of Chemico-Pharmacological Sciences, Graduate School of Pharmaceutical Sciences, Kumamoto University, Kumamoto, Japan; Priority Organization for Innovation and Excellence, Kumamoto University, Kumamoto, Japan; Program for Leading Graduate Schools “HIGO (Health Life Science: Interdisciplinary and Glocal Oriented) Program”, Kumamoto University, Kumamoto, JapanDepartment of Chemico-Pharmacological Sciences, Graduate School of Pharmaceutical Sciences, Kumamoto University, Kumamoto, JapanAutophagy-lysosome proteolysis is classified into macroautophagy (MA), microautophagy (mA) and chaperone-mediated autophagy (CMA). In contrast to MA and CMA, mA have been mainly studied in yeast. In 2011, mammalian mA was identified as a pathway to deliver cytosolic proteins into multivesicular bodies. However, its molecular mechanism is quite different from yeast mA. Using a cell-based method to evaluate mA and CMA, we revealed that rapamycin, an activator of yeast mA, significantly activated mammalian mA. Although rapamycin activates MA, mA was also activated by rapamycin in MA-deficient cells. These findings suggest that rapamycin is a first-identified activator of mammalian mA. Keywords: Microautophagy, Chaperone-mediated autophagy, Rapamycinhttp://www.sciencedirect.com/science/article/pii/S1347861319340629 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Masahiro Sato Takahiro Seki Ayumu Konno Hirokazu Hirai Yuki Kurauchi Akinori Hisatsune Hiroshi Katsuki |
spellingShingle |
Masahiro Sato Takahiro Seki Ayumu Konno Hirokazu Hirai Yuki Kurauchi Akinori Hisatsune Hiroshi Katsuki Rapamycin activates mammalian microautophagy Journal of Pharmacological Sciences |
author_facet |
Masahiro Sato Takahiro Seki Ayumu Konno Hirokazu Hirai Yuki Kurauchi Akinori Hisatsune Hiroshi Katsuki |
author_sort |
Masahiro Sato |
title |
Rapamycin activates mammalian microautophagy |
title_short |
Rapamycin activates mammalian microautophagy |
title_full |
Rapamycin activates mammalian microautophagy |
title_fullStr |
Rapamycin activates mammalian microautophagy |
title_full_unstemmed |
Rapamycin activates mammalian microautophagy |
title_sort |
rapamycin activates mammalian microautophagy |
publisher |
Elsevier |
series |
Journal of Pharmacological Sciences |
issn |
1347-8613 |
publishDate |
2019-06-01 |
description |
Autophagy-lysosome proteolysis is classified into macroautophagy (MA), microautophagy (mA) and chaperone-mediated autophagy (CMA). In contrast to MA and CMA, mA have been mainly studied in yeast. In 2011, mammalian mA was identified as a pathway to deliver cytosolic proteins into multivesicular bodies. However, its molecular mechanism is quite different from yeast mA. Using a cell-based method to evaluate mA and CMA, we revealed that rapamycin, an activator of yeast mA, significantly activated mammalian mA. Although rapamycin activates MA, mA was also activated by rapamycin in MA-deficient cells. These findings suggest that rapamycin is a first-identified activator of mammalian mA. Keywords: Microautophagy, Chaperone-mediated autophagy, Rapamycin |
url |
http://www.sciencedirect.com/science/article/pii/S1347861319340629 |
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