S100A10 Regulates ULK1 Localization to ER–Mitochondria Contact Sites in IFN-γ-Triggered Autophagy

Ying Da Chen; Yi Ting Fang; Chih Peng Chang; Chiou Feng Lin; Li Jin Hsu; Shang Rung Wu; Yen Chi Chiu; Robert Anderson; Yee Shin Lin

doi:10.1016/j.jmb.2016.11.009

S100A10 Regulates ULK1 Localization to ER–Mitochondria Contact Sites in IFN-γ-Triggered Autophagy

Ying Da Chen, Yi Ting Fang, Chih Peng Chang, Chiou Feng Lin, Li Jin Hsu, Shang Rung Wu, Yen Chi Chiu, Robert Anderson, Yee Shin Lin

Medicine

Producción científica: Contribución a una revista › Artículo › revisión exhaustiva

18 Citas (Scopus)

Resumen

During the process of autophagy, the autophagy-related proteins are translocated to autophagosome formation sites. Here, we demonstrate that S100A10 is required for ULK1 localization to autophagosome formation sites. Silencing of S100A10 reduces IFN-γ-induced autophagosome formation. We also determined the role of annexin A2 (ANXA2), a binding partner of S100A10, which has been reported to promote phagophore assembly. Silencing of ANXA2 reduced S100A10 expression. However, overexpression of S100A10 in ANXA2-silenced cells was still able to enhance autophagosome formation, suggesting that ANXA2 regulates IFN-γ-induced autophagy through S100A10. We also observed that S100A10 interacted with ULK1 after IFN-γ stimulation, and S100A10 knockdown prevented ULK1 localization to autophagosome formation sites. Finally, the release of high mobility group protein B1, one of the functions mediated by IFN-γ-induced autophagy, was inhibited in S100A10 knockdown cells. These results elucidate the importance of S100A10 in autophagosome formation and reveal the relationship between S100A10 and ULK1 in IFN-γ-induced autophagy.

Idioma original	English
Páginas (desde-hasta)	142-157
Número de páginas	16
Publicación	Journal of Molecular Biology
Volumen	429
N.º	1
DOI	https://doi.org/10.1016/j.jmb.2016.11.009
Estado	Published - ene. 6 2017

Nota bibliográfica

Funding Information:
This work was supported by Ministry of Science and Technology, Taiwan (grants MOST103-2325-B-006-010 and NSC101-2320-B-006-021-MY3). We thank the National RNAi Core Facility, Academia Sinica, Taipei, Taiwan, for preparing the shRNA and lentivirus vectors. We also thank Professor Tamotsu Yoshimori for providing Myc-ULK1 and GFP-LC3 overexpression plasmids.

Publisher Copyright:
© 2016

ASJC Scopus Subject Areas

Biophysics
Structural Biology
Molecular Biology

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title = "S100A10 Regulates ULK1 Localization to ER–Mitochondria Contact Sites in IFN-γ-Triggered Autophagy",

abstract = "During the process of autophagy, the autophagy-related proteins are translocated to autophagosome formation sites. Here, we demonstrate that S100A10 is required for ULK1 localization to autophagosome formation sites. Silencing of S100A10 reduces IFN-γ-induced autophagosome formation. We also determined the role of annexin A2 (ANXA2), a binding partner of S100A10, which has been reported to promote phagophore assembly. Silencing of ANXA2 reduced S100A10 expression. However, overexpression of S100A10 in ANXA2-silenced cells was still able to enhance autophagosome formation, suggesting that ANXA2 regulates IFN-γ-induced autophagy through S100A10. We also observed that S100A10 interacted with ULK1 after IFN-γ stimulation, and S100A10 knockdown prevented ULK1 localization to autophagosome formation sites. Finally, the release of high mobility group protein B1, one of the functions mediated by IFN-γ-induced autophagy, was inhibited in S100A10 knockdown cells. These results elucidate the importance of S100A10 in autophagosome formation and reveal the relationship between S100A10 and ULK1 in IFN-γ-induced autophagy.",

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note = "Funding Information: This work was supported by Ministry of Science and Technology, Taiwan (grants MOST103-2325-B-006-010 and NSC101-2320-B-006-021-MY3). We thank the National RNAi Core Facility, Academia Sinica, Taipei, Taiwan, for preparing the shRNA and lentivirus vectors. We also thank Professor Tamotsu Yoshimori for providing Myc-ULK1 and GFP-LC3 overexpression plasmids. Publisher Copyright: {\textcopyright} 2016",

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AU - Lin, Chiou Feng

AU - Hsu, Li Jin

AU - Wu, Shang Rung

AU - Chiu, Yen Chi

AU - Anderson, Robert

AU - Lin, Yee Shin

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PY - 2017/1/6

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N2 - During the process of autophagy, the autophagy-related proteins are translocated to autophagosome formation sites. Here, we demonstrate that S100A10 is required for ULK1 localization to autophagosome formation sites. Silencing of S100A10 reduces IFN-γ-induced autophagosome formation. We also determined the role of annexin A2 (ANXA2), a binding partner of S100A10, which has been reported to promote phagophore assembly. Silencing of ANXA2 reduced S100A10 expression. However, overexpression of S100A10 in ANXA2-silenced cells was still able to enhance autophagosome formation, suggesting that ANXA2 regulates IFN-γ-induced autophagy through S100A10. We also observed that S100A10 interacted with ULK1 after IFN-γ stimulation, and S100A10 knockdown prevented ULK1 localization to autophagosome formation sites. Finally, the release of high mobility group protein B1, one of the functions mediated by IFN-γ-induced autophagy, was inhibited in S100A10 knockdown cells. These results elucidate the importance of S100A10 in autophagosome formation and reveal the relationship between S100A10 and ULK1 in IFN-γ-induced autophagy.

AB - During the process of autophagy, the autophagy-related proteins are translocated to autophagosome formation sites. Here, we demonstrate that S100A10 is required for ULK1 localization to autophagosome formation sites. Silencing of S100A10 reduces IFN-γ-induced autophagosome formation. We also determined the role of annexin A2 (ANXA2), a binding partner of S100A10, which has been reported to promote phagophore assembly. Silencing of ANXA2 reduced S100A10 expression. However, overexpression of S100A10 in ANXA2-silenced cells was still able to enhance autophagosome formation, suggesting that ANXA2 regulates IFN-γ-induced autophagy through S100A10. We also observed that S100A10 interacted with ULK1 after IFN-γ stimulation, and S100A10 knockdown prevented ULK1 localization to autophagosome formation sites. Finally, the release of high mobility group protein B1, one of the functions mediated by IFN-γ-induced autophagy, was inhibited in S100A10 knockdown cells. These results elucidate the importance of S100A10 in autophagosome formation and reveal the relationship between S100A10 and ULK1 in IFN-γ-induced autophagy.

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S100A10 Regulates ULK1 Localization to ER–Mitochondria Contact Sites in IFN-γ-Triggered Autophagy

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