Stress-induced proteome remodeling at the Golgi–endosome interface

Cellular stress response pathways support cell survival under stress and are often leveraged by cancer cells to gain advantageous traits. How cells respond to Golgi stress is incompletely understood, limiting insights into the role of Golgi stress in cancer. Here, we combined small-molecule stress models and proteomic analyses to elucidate stress-induced changes at the Golgi. Our data establish the depletion of Golgi transport proteins as a common response to different Golgi stressors, including ionophores and oxysterol-binding protein (OSBP) inhibitors. Ionophores further induce de novo expression of the stress response protein FAM129A (also known as NIBAN1), which localizes to the remodeled secretory pathway. In a group of melanoma cells, displaying a dedifferentiated epithelial-to-mesenchymal-transition (EMT)-like phenotype, FAM129A is constitutively expressed. In these cells, stress-induced localization of FAM129A to the secretory pathway is achieved by relocalization from the plasma membrane. Collectively, our data highlight the Golgi-endosome interface as a critical hub of the cellular response to Golgi stress and reveal cancer cell-specific effects of this response.

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Publication Details

Journal
Journal of Cell Science
Published
2026-04-16
DOI
https://doi.org/10.1242/jcs.264535
Primary Topic
Cellular transport and secretion
Type
article
Field-Weighted Citation Impact
0.00

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article

Stress-induced proteome remodeling at the Golgi–endosome interface

Doris Hellerschmied, Michelle Koci, Markus Kaiser, Jasmin Schillinger et al.
Journal of Cell Science
Cellular transport and secretion
article

Stress-induced proteome remodeling at the Golgi–endosome interface

Doris Hellerschmied, Michelle Koci, Markus Kaiser, Jasmin Schillinger, Philine Steinbach, Annette Paschen, Sabrina Ninck, Simone Stupia, Beatrice Thier, Farnusch Kaschani, Lana Buzuk, Savina Abraham Pol, Gina Simon, Melisa Dendusic, Hai Trinh, Nina Schulze, Michael Ehrmann
article en

Abstract

Cellular stress response pathways support cell survival under stress and are often leveraged by cancer cells to gain advantageous traits. How cells respond to Golgi stress is incompletely understood, limiting insights into the role of Golgi stress in cancer. Here, we combined small-molecule stress models and proteomic analyses to elucidate stress-induced changes at the Golgi. Our data establish the depletion of Golgi transport proteins as a common response to different Golgi stressors, including ionophores and oxysterol-binding protein (OSBP) inhibitors. Ionophores further induce de novo expression of the stress response protein FAM129A (also known as NIBAN1), which localizes to the remodeled secretory pathway. In a group of melanoma cells, displaying a dedifferentiated epithelial-to-mesenchymal-transition (EMT)-like phenotype, FAM129A is constitutively expressed. In these cells, stress-induced localization of FAM129A to the secretory pathway is achieved by relocalization from the plasma membrane. Collectively, our data highlight the Golgi-endosome interface as a critical hub of the cellular response to Golgi stress and reveal cancer cell-specific effects of this response.

Journal of Cell ScienceVol. 139(9)
Essen University Hospital (DE), German Marine Research Consortium (DE), Institute of Cell Biology (UA), Pharmaceutical Biotechnology (Czechia) (CZ), University of Duisburg-Essen (DE)
Alexander von Humboldt-Stiftung, Deutsche Forschungsgemeinschaft, Universität Duisburg-Essen
Good health and well-being
Openalex Percentile: Top 25%
Cellular transport and secretion
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