| Title | A new type of ERGIC-ERES membrane contact mediated by TMED9 and SEC12 is required for autophagosome biogenesis |
| Authors | Li, Shulin Yan, Rui Xu, Jialu Zhao, Shiqun Ma, Xinyu Sun, Qiming Zhang, Min Li, Ying Liu, Jun-Jie Gogo Chen, Liangyi Li, Sai Xu, Ke Ge, Liang |
| Affiliation | State Key Lab Membrane Biol, Beijing, Peoples R China Tsinghua Peking Ctr Life Sci, Beijing, Peoples R China Tsinghua Univ, Sch Life Sci, Beijing, Peoples R China Univ Calif Berkeley, Dept Chem, Berkeley, CA 94720 USA Beijing Adv Innovat Ctr Struct Biol, Beijing, Peoples R China Peking Univ, Inst Mol Med, Beijing Key Lab Cardiometab Mol Med, Beijing, Peoples R China Natl Ctr Nanosci & Technol, Beijing, Peoples R China Zhejiang Univ, Dept Cardiol, Dept Biochem, Affiliated Hosp 2,Sch Med, Hangzhou, Zhejiang, Peoples R China |
| Keywords | EXIT SITES ENDOPLASMIC-RETICULUM LC3 LIPIDATION PROTEIN TRANSPORT COPII IDENTIFICATION NETWORK PATHWAY COMPLEX |
| Issue Date | Sep-2021 |
| Publisher | CELL RESEARCH |
| Abstract | Under stress, the endomembrane system undergoes reorganization to support autophagosome biogenesis, which is a central step in autophagy. How the endomembrane system remodels has been poorly understood. Here we identify a new type of membrane contact formed between the ER-Golgi intermediate compartment (ERGIC) and the ER-exit site (ERES) in the ER-Golgi system, which is essential for promoting autophagosome biogenesis induced by different stress stimuli. The ERGIC-ERES contact is established by the interaction between TMED9 and SEC12 which generates a short distance opposition (as close as 2-5 nm) between the two compartments. The tight membrane contact allows the ERES-located SEC12 to transactivate COPII assembly on the ERGIC. In addition, a portion of SEC12 also relocates to the ERGIC. Through both mechanisms, the ERGIC-ERES contact promotes formation of the ERGIC-derived COPII vesicle, a membrane precursor of the autophagosome. The ERGIC-ERES contact is physically and functionally different from the TFG-mediated ERGIC-ERES adjunction involved in secretory protein transport, and therefore defines a unique endomembrane structure generated upon stress conditions for autophagic membrane formation. |
| URI | http://hdl.handle.net/20.500.11897/626093 |
| ISSN | 1001-0602 |
| DOI | 10.1038/s41422-021-00563-0 |
| Indexed | SCI(E) |
| Appears in Collections: | 分子医学研究所 |
