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

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dc.contributor.authorSong, Min Seok-
dc.contributor.authorSim, Hun Ju-
dc.contributor.authorEun, Sung Ho-
dc.contributor.authorJung, Min Kyo-
dc.contributor.authorHwang, Su Jin-
dc.contributor.authorHam, Min Hee-
dc.contributor.authorKwak, Kihyuck-
dc.contributor.authorLee, Hea Ji-
dc.contributor.authorKim, Jin Young-
dc.contributor.authorJang, Dong Geon-
dc.contributor.authorChung, Hee Chun-
dc.contributor.authorShin, Dong Hoon-
dc.contributor.authorKim, Ye Jin-
dc.contributor.authorNoh, Shin Hye-
dc.contributor.authorMun, Ji Young-
dc.contributor.authorLee, Jae Myun-
dc.contributor.authorLee, Min Goo-
dc.date.accessioned2025-02-12T06:00:17Z-
dc.date.available2025-02-12T06:00:17Z-
dc.date.issued2025-02-
dc.identifier.issn1534-5807-
dc.identifier.issn1878-1551-
dc.identifier.urihttp://scholarworks.bwise.kr/kbri/handle/2023.sw.kbri/1240-
dc.description.abstractCellular 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.-
dc.publisherCell Press-
dc.titleTubular ER structures shaped by ER-phagy receptors engage in stress-induced Golgi bypass-
dc.typeArticle-
dc.publisher.location미국-
dc.identifier.doi10.1016/j.devcel.2025.01.011-
dc.identifier.bibliographicCitationDevelopmental Cell-
dc.citation.titleDevelopmental Cell-
dc.description.isOpenAccessN-
dc.description.journalRegisteredClassscie-
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