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Tubular ER structures shaped by ER-phagy receptors engage in stress-induced Golgi bypass

Authors
Song, Min SeokSim, Hun JuEun, Sung HoJung, Min KyoHwang, Su JinHam, Min HeeKwak, KihyuckLee, Hea JiKim, Jin YoungJang, Dong GeonChung, Hee ChunShin, Dong HoonKim, Ye JinNoh, Shin HyeMun, Ji YoungLee, Jae MyunLee, Min Goo
Issue Date
Feb-2025
Publisher
Cell Press
Citation
Developmental Cell
Journal Title
Developmental Cell
URI
http://scholarworks.bwise.kr/kbri/handle/2023.sw.kbri/1240
DOI
10.1016/j.devcel.2025.01.011
ISSN
1534-5807
1878-1551
Abstract
Cellular stresses, particularly endoplasmic reticulum (ER) stress induced by ER-to-Golgi transport blockade, trigger Golgi-independent secretion of cytosolic and transmembrane proteins. However, the molecular mechanisms underlying this unconventional protein secretion (UPS) remain largely elusive. Here, we report that an ER tubulovesicular structure (ER tubular body [ER-TB]), shaped by the tubular ER-phagy receptors ATL3 and RTN3L, plays an important role in stress-induced UPS of transmembrane proteins such as cystic fibrosis transmembrane conductance regulator (CFTR) and severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike protein. Correlative light-electron microscopy analyses demonstrate the formation of ER-TB under UPS-inducing conditions in HEK293 and HeLa cells. Individual gene knockdowns of ATL3 and RTN3 inhibit ER-TB formation and the UPS of trafficking-deficient ΔF508-CFTR. Combined supplementation of ATL3 and RTN3L induces ER-TB formation and UPS. ATL3 also participates in the SARS-CoV-2-associated convoluted membrane formation and Golgi-independent trafficking of SARS-CoV-2 spike protein. These findings suggest that ER-TB serves a common function in mediating stress-induced UPS, which participates in various physiological and pathophysiological processes.
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