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

Authors
 Min Seok Song  ;  Hun Ju Sim  ;  Sung Ho Eun  ;  Min Kyo Jung  ;  Su Jin Hwang  ;  Min Hee Ham  ;  Kihyuck Kwak  ;  Hea Ji Lee  ;  Jin Young Kim  ;  Dong Geon Jang  ;  Hee Chun Chung  ;  Dong Hoon Shin  ;  Ye Jin Kim  ;  Shin Hye Noh  ;  Ji Young Mun  ;  Jae Myun Lee  ;  Min Goo Lee 
Citation
 DEVELOPMENTAL CELL, Vol.60(11) : 1568-1585.e11, 2025-06 
Journal Title
DEVELOPMENTAL CELL
ISSN
 1534-5807 
Issue Date
2025-06
MeSH
1
Keywords
COVID-19 / metabolism ; COVID-19 / virology ; Carrier Proteins / metabolism ; Cystic Fibrosis Transmembrane Conductance Regulator / genetics ; Cystic Fibrosis Transmembrane Conductance Regulator / metabolism ; Endoplasmic Reticulum Stress* / physiology ; Endoplasmic Reticulum* / metabolism ; Endoplasmic Reticulum* / ultrastructure ; Golgi Apparatus* / metabolism ; HEK293 Cells ; HeLa Cells ; Humans ; Membrane Proteins* / genetics ; Membrane Proteins* / metabolism ; Nerve Tissue Proteins* / genetics ; Nerve Tissue Proteins* / metabolism ; Protein Transport ; SARS-CoV-2 / metabolism ; Spike Glycoprotein, Coronavirus / metabolism
Abstract
ATL3; ER stress; ER tubular body; RTN3; unconventional protein secretion
Article Number
 10.1016/j.devcel.2025.01.011 
DOI
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.
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Microbiology (미생물학교실) > 1. Journal Papers
1. College of Medicine (의과대학) > BioMedical Science Institute (의생명과학부) > 1. Journal Papers
1. College of Medicine (의과대학) > Dept. of Pharmacology (약리학교실) > 1. Journal Papers
Yonsei Authors
Kwak, Kihyuck(곽기혁)
Noh, Shin Hye(노신혜) ORCID logo https://orcid.org/0000-0003-3118-9240
Shin, Dong Hoon(신동훈)
Lee, Min Goo(이민구) ORCID logo https://orcid.org/0000-0001-7436-012X
Lee, Jae Myun(이재면) ORCID logo https://orcid.org/0000-0002-5273-3113
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/207450
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