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

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• 作者：Ying-Da Chen¹ ; Yi-Ting Fang² ; Chih-Peng Chang¹ ; ² ; ³ ; Chiou-Feng Lin³ ; ⁴ ; Li-Jin Hsu¹ ; ³ ; ⁵ ; Shang-Rung Wu⁶ ; Yen-Chi Chiu⁶ ; Robert Anderson⁷ ; Yee-Shin Lin¹ ; ² ; ³ ; ^{yslin1@mail.ncku.edu.tw}
• 关键词：ANXA2 ; annexin A2 ; ATG ; autophagy-related ; BECN1 ; Beclin 1 ; CANX ; calnexin ; CTSS ; cathepsin S ; ER ; endoplasmic reticulum ; HMGB1 ; high mobility group protein B1 ; HRP ; horseradish peroxidase ; MTOR ; mechanistic target of rapamycin ; PI3K ; phosphatidylinositol 3-kinase ; RFP ; red fluorescent protein ; shRNA ; short hairpin RNA ; TASK-1 ; two-pore-domain acid-sensitive K+ channel-1 ; TOMM20 ; translocase of outer mitochondrial membrane 20 homolog ; ULK1 ; unc-51 like autophagy activating kinase 1
• 刊名：Journal of Molecular Biology
• 出版年：2017
• 出版时间：6 January 2017
• 年：2017
• 卷：429
• 期：1
• 页码：142-157
• 全文大小：2448 K
• 卷排序：429

文摘

This study demonstrates a role for S100A10 in autophagy. Silencing of S100A10 reduces IFN-γ-induced autophagosome formation. S100A10 interacts and regulates ULK1 localization to endoplasmic reticulum–mitochondria contact sites. S100A10 regulates autophagy-dependent high mobility group protein B1 release. Our study reveals a regulatory role for S100A10 on ULK1 in IFN-γ-induced autophagy.