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IRE1-RACK1 axis orchestrates ER stress preconditioning-elicited cytoprotection from ischemia/reperfusion injury in liver

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分子细胞生物学报:英文版 2016年第2期8卷 144-156页

作者： Dong Liu Xing Liu Ti Zhou William Yao Jun Zhao Zhigang Zheng Wei Jiang Fengsong Wang Felix O.Aikhionbare Donald L.Hill nerimah emmett Zhen Guo Dongmei Wang Xuebiao Yao Yong Chen Department of Hepatobiliary Surgery Xijing HospitalFourth Military Medical UniversityXi’an 710032China Anhui Key Laboratory of Cellular Dynamics and Hefei National Laboratory for Physical Sciences at Nanoscale Hefei 230027China Atlanta Clinical&Translational Science Institute AtlantaGA 30310USA Department of Pathology Xijing HospitalFourth Military Medical UniversityXi’an 710032China Department of Biochemistry Anhui Medical UniversityHefei 230027China Comprehensive Cancer Center University of Alabama at BirminghamBirminghamAL 35294USA Department of Hepatobiliary Surgery Navy General HospitalBeijing 100048China

Endoplasmic reticulum(ER)stress is involved in ischemic preconditioning that protects various organs from ischemia/reperfusion(I/R)*** established an in vivo ER stress preconditioning model in which tunicamycin was injected into rats before hepatic I/*** hepatic I/R injury,demonstrated by serum aminotransferase level and the ultra-structure of the liver,was alleviated by administration of tunicamycin,which induced ER stress in rat liver by activating inositol-requiring enzyme1(IRE1)andupregulating78 kDaglucose-regulated protein(GRP78).The proteomic identification for IRE1 binders revealed interaction and cooperation among receptor for activated C kinase 1(RACK1),phosphorylated AMPK,and IRE1 under ER stress conditions in a spatiotemporal ***,in vitro ER stress preconditioningwas induced by thapsigargin and tunicamycin in L02 and Hep G2 ***,BCL2 was found to bephosphorylated by IRE1 under ER stress conditions to prevent apoptotic process by activation of *** conclusion,ER stress preconditioning protects against hepatic I/R injury,which is orchestrated by IRE1-RACK1 axis through the activation of *** findings provide novel insights into the molecular pathways underlying ER stress preconditioning-elicited cytoprotective effect against hepatic I/R injury.

关键词： IRE1 RACK1 AMPK BCL2 ER stress preconditioning ischemia/reperfusion injury

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Acetylation of ezrin regulates membrane–cytoskeleton interaction underlying CCL18-elicited cell migration

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Journal of Molecular Cell Biology 2020年第6期12卷 424-437页

作者： Xiaoyu Song Wanjuan Wang Haowei Wang Xiao Yuan Fengrui Yang Lingli Zhao McKay Mullen Shihao Du Najdat Zohbi Saravanakumar Muthusamy Yalei Cao Jiying Jiang Peng Xia Ping He Mingrui Ding nerimah emmett Mingming Ma Quan Wu Hadiyah-Nicole Green Xia Ding Dongmei Wang Fengsong Wang Xing Liu School of Traditional Medicine Beijing University of Chinese MedicineBeijingChina MOE Key Laboratory for Membraneless Organelles&Cellular Dynamics Hefei National Center for Physical Sciences at the MicroscaleHefeiChina Morehouse School of Medicine Keck Center for Organoids PlasticityAtlantaGAUSA Optics and Optical Engineering University of Science and Technology of ChinaHefeiChina School of Life Science Anhui Medical UniversityHefeiChina

Ezrin,a membrane–cytoskeleton linker protein,plays an essential role in cell polarity establishment,cell migration,and *** studies show that ezrin phosphorylation regulates breast cancer metastasis by promoting cancer cell survivor and promotes intrahepatic metastasis via cell ***,it was less characterized whether there are additional post-translational modifications and/or post-translational crosstalks on ezrin underlying context-dependent breast cancer cell migration and *** we show that ezrin is acetylated by p300/CBP-associated factor(PCAF)in breast cancer cells in response to CCL18 *** physically interacts with PCAF and is a cognate substrate of *** acetylation site of ezrin was mapped by mass spectrometric analyses,and dynamic acetylation of ezrin is essential for CCL18-induced breast cancer cell migration and ***,the acetylation reduced the lipid-binding activity of ezrin to ensure a robust and dynamic cycling between the plasma membrane and cytosol in response to CCL18 *** analyses show that ezrin acetylation prevents the phosphorylation of *** atomic force microscopic measurements,our study revealed that acetylation of ezrin induced its unfolding into a dominant structure,which prevents ezrin phosphorylation at ***,these results present a previously undefined mechanism by which CCL18-elicited crosstalks between the acetylation and phosphorylation on ezrin control breast cancer cell migration and *** suggests that targeting PCAF signaling could be a potential therapeutic strategy for combating hyperactive ezrin-driven cancer progression.

关键词： ezrin acetylation phosphorylation actin cell migration

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LRIF1 interacts with HPla to coordinate accurate chromosome segregation during mitosis

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Journal of Molecular Cell Biology 2018年第6期10卷 527-538页

作者： Saima Akram Fengrui Yang Junying Li Gregory Adams Yingying Liu Xiaoxuan Zhuang Lingluo Chu Xu Liu nerimah emmett Winston Thompson McKay Mullen Saravana Muthusamy Wenwen Wang Fei Mo Xing Liu Anhui Key Laboratory for Cellular Dynamics University of Science &Technology of China School of Life SciencesNational Science Center for Physical Sciences at Nanoscaleand Chinese Academy of Science Center of Excellence on Molecular Cell SciencesHefei 230027China Keck Center for Molecular Imaging Department of PhysiologyMorehouse School of MedicineAtlantaGA 30310USA National Institutes of Health BethesdaMD 20892USA Department of Molecular Cell Biology Harvard UniversityCambridgeMA 02138USA

Heterochromatin protein 1α (HP1α)regulates chromatin specification and plasticity during cell fate *** structural determinants account for HP1α Localization and function during cell division *** earlier study showed that centromeric Localization of HP1α depends on the epigenetic mark H3K9me3 in interphase,while its centromeric location in mitosis relies on uncharacterized PXVXL-containing ***,we identified a PXVXL-containing protein,Ligand-dependent nuclear receptorinteracting factor 1 (LRIF1),which recruits HPla to the centromere of mitotic chromosomes and its interaction with HP1α is essential for accurate chromosome segregation during ***1 interacts directly with HPla chromoshadow domain via an evolutionariLy conserved PXVXL motif within its ***,the LRIF1-HPla interaction is critical for Aurora B activity in the inner *** of PXVXL motif of LRIF1 Leads to defects in HPla centromere targeting and aberrant chromosome *** findings reveal a previously unrecognized direct Link between LRIF1 and HP1α in centromere plasticity control and illustrate the critical role of LRIF1-HP1α interaction in orchestrating accurate cell division.

关键词： HP1α LRIF1 mitosis centromere chromosome segregation

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