2024年6月3日 / 最終更新日 : 2024年7月22日 ad_y ニュース

2024年 新着論文 32　細胞情報学分野から論文が発表されました

YIPF3 and YIPF4 regulate autophagic turnover of the Golgi apparatus

EMBO J. 2024 Jul;43(14):2954-2978. doi: 10.1038/s44318-024-00131-3. Epub 2024 May 31.

Authors

Shinri Kitta  1 , Tatsuya Kaminishi  1   2 , Momoko Higashi  3 , Takayuki Shima  1 , Kohei Nishino  4 , Nobuhiro Nakamura  5 , Hidetaka Kosako  4 , Tamotsu Yoshimori  6   7   8 , Akiko Kuma  9   10

Affiliations

  • 1 Department of Genetics, Graduate School of Medicine, Osaka University, Suita, Osaka, 565-0871, Japan.
  • 2 Integrated Frontier Research for Medical Science Division, Institute for Open and Transdisciplinary Research Initiatives (OTRI), Osaka University, Suita, Osaka, 565-0871, Japan.
  • 3 Laboratory of Intracellular Membrane Dynamics, Graduate School of Frontier Biosciences, Osaka University, Suita, Osaka, 565-0871, Japan.
  • 4 Division of Cell Signaling, Fujii Memorial Institute of Medical Sciences, Institute of Advanced Medical Sciences, Tokushima University, Tokushima, 770-8503, Japan.
  • 5 Faculty of Life Sciences, Kyoto Sangyo University, Motoyama, Kamigamo, Kita, Kyoto, 603-8555, Japan.
  • 6 Department of Genetics, Graduate School of Medicine, Osaka University, Suita, Osaka, 565-0871, Japan. tamyoshi@fbs.osaka-u.ac.jp.
  • 7 Integrated Frontier Research for Medical Science Division, Institute for Open and Transdisciplinary Research Initiatives (OTRI), Osaka University, Suita, Osaka, 565-0871, Japan. tamyoshi@fbs.osaka-u.ac.jp.
  • 8 Laboratory of Intracellular Membrane Dynamics, Graduate School of Frontier Biosciences, Osaka University, Suita, Osaka, 565-0871, Japan. tamyoshi@fbs.osaka-u.ac.jp.
  • 9 Department of Genetics, Graduate School of Medicine, Osaka University, Suita, Osaka, 565-0871, Japan. kuma@fbs.osaka-u.ac.jp.
  • 10 Department of Biochemistry and Molecular Biology, Graduate School of Medicine, The University of Tokyo, Bunkyo-ku, Tokyo, 113-0033, Japan. kuma@fbs.osaka-u.ac.jp.

Abstract

The degradation of organelles by autophagy is essential for cellular homeostasis. The Golgi apparatus has recently been demonstrated to be degraded by autophagy, but little is known about how the Golgi is recognized by the forming autophagosome. Using quantitative proteomic analysis and two novel Golgiphagy reporter systems, we found that the five-pass transmembrane Golgi-resident proteins YIPF3 and YIPF4 constitute a Golgiphagy receptor. The interaction of this complex with LC3B, GABARAP, and GABARAPL1 is dependent on a LIR motif within YIPF3 and putative phosphorylation sites immediately upstream; the stability of the complex is governed by YIPF4. Expression of a YIPF3 protein containing a mutated LIR motif caused an elongated Golgi morphology, indicating the importance of Golgi turnover via selective autophagy. The reporter assays reported here may be readily adapted to different experimental contexts to help deepen our understanding of Golgiphagy.

Keywords: Autophagy Receptor; Golgi Turnover; Golgiphagy; Organelle Degradation; Selective Autophagy.

Conflict of interest statement

The authors declare no competing interests.

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