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Discovery of Atg5/Atg7-independent alternative macroautophagy

Author

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  • Yuya Nishida

    (Medical Research Institute, Tokyo Medical and Dental University, 1-5-45 Yushima, Bunkyo-ku, Tokyo 113-8510, Japan
    Department of Medical Genetics,)

  • Satoko Arakawa

    (Medical Research Institute, Tokyo Medical and Dental University, 1-5-45 Yushima, Bunkyo-ku, Tokyo 113-8510, Japan)

  • Kenji Fujitani

    (Medical Research Institute, Tokyo Medical and Dental University, 1-5-45 Yushima, Bunkyo-ku, Tokyo 113-8510, Japan)

  • Hirofumi Yamaguchi

    (Medical Research Institute, Tokyo Medical and Dental University, 1-5-45 Yushima, Bunkyo-ku, Tokyo 113-8510, Japan)

  • Takeshi Mizuta

    (Medical Research Institute, Tokyo Medical and Dental University, 1-5-45 Yushima, Bunkyo-ku, Tokyo 113-8510, Japan)

  • Toku Kanaseki

    (Medical Research Institute, Tokyo Medical and Dental University, 1-5-45 Yushima, Bunkyo-ku, Tokyo 113-8510, Japan)

  • Masaaki Komatsu

    (Laboratory of Frontier Science, Tokyo Metropolitan Institute of Medical Science, Bunkyo-ku, Tokyo 113-8613, Japan)

  • Kinya Otsu

    (Osaka University Medical School, 2-2 Yamadaoka, Suita, Osaka 565-0871, Japan)

  • Yoshihide Tsujimoto

    (Department of Medical Genetics,)

  • Shigeomi Shimizu

    (Medical Research Institute, Tokyo Medical and Dental University, 1-5-45 Yushima, Bunkyo-ku, Tokyo 113-8510, Japan)

Abstract

A second type of macroautophagy In a process known as macroautophagy, defective proteins and entire organelles are sequestered in membrane compartments called autophagosomes that ultimately fuse with lysososmes and undergo degradation. This pathway is activated in response to conditions such as starvation, allowing a cell to break up its own reserves to provide nutrients. At the molecular level, macroautophagy is regulated by Atg genes that are components of the ubiquitin-like conjugation system. Nishida et al. describe a second mode of autophagy that is independent of the Atg genes and is induced under certain stress conditions in vitro and in the clearance of organelles during erythroid maturation in vivo. Future studies will reveal the mechanistic basis for this pathway.

Suggested Citation

  • Yuya Nishida & Satoko Arakawa & Kenji Fujitani & Hirofumi Yamaguchi & Takeshi Mizuta & Toku Kanaseki & Masaaki Komatsu & Kinya Otsu & Yoshihide Tsujimoto & Shigeomi Shimizu, 2009. "Discovery of Atg5/Atg7-independent alternative macroautophagy," Nature, Nature, vol. 461(7264), pages 654-658, October.
    • Handle: RePEc:nat:nature:v:461:y:2009:i:7264:d:10.1038_nature08455
    DOI: 10.1038/nature08455
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    Cited by:

    1. Hayden Weng Siong Tan & Guang Lu & Han Dong & Yik-Lam Cho & Auginia Natalia & Liming Wang & Charlene Chan & Dennis Kappei & Reshma Taneja & Shuo-Chien Ling & Huilin Shao & Shih-Yin Tsai & Wen-Xing Din, 2022. "A degradative to secretory autophagy switch mediates mitochondria clearance in the absence of the mATG8-conjugation machinery," Nature Communications, Nature, vol. 13(1), pages 1-17, December.
    2. Shuzhi Cui & Tian Xia & Jianjin Zhao & Xiaoyu Ren & Tingtao Wu & Mireille Kameni & Xiaoju Guo & Li He & Jingao Guo & Aléria Duperray-Susini & Florence Levillayer & Jean-Marc Collard & Jin Zhong & Life, 2023. "NDP52 mediates an antiviral response to hepatitis B virus infection through Rab9-dependent lysosomal degradation pathway," Nature Communications, Nature, vol. 14(1), pages 1-16, December.

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