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

研究成果: Article

3 引文 (Scopus)

摘要

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.

原文English
頁(從 - 到)142-157
頁數16
期刊Journal of Molecular Biology
429
發行號1
DOIs
出版狀態Published - 2017 一月 6

指紋

Autophagy
Annexin A2
High Mobility Group Proteins
Annexins
Autophagosomes

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Molecular Biology

引用此文

Chen, Ying Da ; Fang, Yi Ting ; Chang, Chih Peng ; Lin, Chiou Feng ; Hsu, Li Jin ; Wu, Shang Rung ; Chiu, Yen Chi ; Anderson, Robert ; Lin, Yee Shin. / S100A10 Regulates ULK1 Localization to ER–Mitochondria Contact Sites in IFN-γ-Triggered Autophagy. 於: Journal of Molecular Biology. 2017 ; 卷 429, 編號 1. 頁 142-157.
@article{6a5b611d40b349a695b5e4d24d8aac91,
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.",
author = "Chen, {Ying Da} and Fang, {Yi Ting} and Chang, {Chih Peng} and Lin, {Chiou Feng} and Hsu, {Li Jin} and Wu, {Shang Rung} and Chiu, {Yen Chi} and Robert Anderson and Lin, {Yee Shin}",
year = "2017",
month = "1",
day = "6",
doi = "10.1016/j.jmb.2016.11.009",
language = "English",
volume = "429",
pages = "142--157",
journal = "Journal of Molecular Biology",
issn = "0022-2836",
publisher = "Academic Press Inc.",
number = "1",

}

S100A10 Regulates ULK1 Localization to ER–Mitochondria Contact Sites in IFN-γ-Triggered Autophagy. / Chen, Ying Da; Fang, Yi Ting; Chang, Chih Peng; Lin, Chiou Feng; Hsu, Li Jin; Wu, Shang Rung; Chiu, Yen Chi; Anderson, Robert; Lin, Yee Shin.

於: Journal of Molecular Biology, 卷 429, 編號 1, 06.01.2017, p. 142-157.

研究成果: Article

TY - JOUR

T1 - S100A10 Regulates ULK1 Localization to ER–Mitochondria Contact Sites in IFN-γ-Triggered Autophagy

AU - Chen, Ying Da

AU - Fang, Yi Ting

AU - Chang, Chih Peng

AU - Lin, Chiou Feng

AU - Hsu, Li Jin

AU - Wu, Shang Rung

AU - Chiu, Yen Chi

AU - Anderson, Robert

AU - Lin, Yee Shin

PY - 2017/1/6

Y1 - 2017/1/6

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.

UR - http://www.scopus.com/inward/record.url?scp=85006975370&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85006975370&partnerID=8YFLogxK

U2 - 10.1016/j.jmb.2016.11.009

DO - 10.1016/j.jmb.2016.11.009

M3 - Article

C2 - 27871932

AN - SCOPUS:85006975370

VL - 429

SP - 142

EP - 157

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

SN - 0022-2836

IS - 1

ER -