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GTPase Activity of MxB Contributes to Its Nuclear Location, Interaction with nucleoporins and Anti-HIV-1 Activity

Virologica Sinica 2021年第1期36卷 85-94页

作者： Linlin Xie Zhao Ju Chaojie Zhong Yingjun Wu Yuxing Zan Wei Hou Yong Feng State Key Laboratory of Virology/Institute of Medical Virology/Hubei Province Key Laboratory of Allergy and Immunology School of Basic Medical SciencesWuhan UniversityWuhan 430071China

The human myxovirus resistance 2(Mx2/Mx B)protein,a member of interferon(IFN)-inducible dynamin-like large GTPases,restricts a number of virus *** of these viruses occurs at poorly-defined steps after viral entry and has a common requirement for Mx B ***,the GTPase activity is essential for the anti-viral effects of Mx B against herpesviruses and HBV but not *** understand the role of Mx B GTPase activity,including GTP binding and GTP hydrolysis,in restriction of HIV-1 infection,we genetically separated these two functions and evaluated their contributions to *** found that both the GTP binding and hydrolysis function of Mx B involved in the restriction of HIV-1 *** GTPase activity of Mx B contributed to its nuclear location,interaction with nucleoporins(NUPs)and HIV-1 ***,Mx B disrupted the association between NUPs and HIV-1 cores dependently upon its GTPase *** function of GTPase activity was therefore multi-faceted,led to fundamentally distinct mechanisms employed by wild-type Mx B and GTPase activity defective Mx B mutations to restrict HIV-1 replication.

关键词： Human immunodeficiency virus type 1(HIV-1) Human myxovirus resistance 2(MxB) GTPase activity nucleoporin Capsid(CA) Anti-viral activity

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Post-translational O-GlcNAcylation is essential for nuclear pore integrity and maintenance of the pore selectivity filter

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Journal of Molecular Cell Biology 2016年第1期8卷 2-16页

作者： Yanping Zhu Ta-Wei Liu Zarina Madden Scott A.Yuzwa Kelsey Murray Samy Cecioni Natasha Zachara David J.Vocadlo Department of Chemistry Simon Fraser UniversityBurnabyBritish Columbia V5A 1S6Canada Department of Molecular Biology and Biochemistry Simon Fraser UniversityBurnabyBritish Columbia V5A 1S6Canada Department of Biological Chemistry Johns Hopkins University Medical SchoolBaltimoreMD 21205USA

O-glycosylation of the nuclear pore complex(NPC)by O-linked N-acetylglucosamine(O-GlcNAc)is conserved within *** nucleoporins(Nups)comprising the NPC are constitutively O-GlcNAcylated,but the functional role of this modification remains *** loss ofO-GlcNAc,induced by either inhibition ofO-GlcNAc transferase(OGT)or deletion of the gene encoding OGT,leads to decreased cellular levels of a number of natively O-GlcNAcylated *** of O-GlcNAc enables increased ubiquitination of these Nups and their increased proteasomal *** decreased half-life of these deglycosylated Nups manifests in their gradual loss from the NPC and a downstream malfunction of the nuclear pore selective permeability barrier in both dividing and post-mitotic *** findings define a critical role of O-GlcNAc modification of the NPC in maintaining its composition and the function of the selectivity *** results implicate NPC glycosylation as a regulator of NPC function and reveal the role of conserved glycosylation of the NPC among metazoans.

关键词： post-translational modiﬁcation O-GlcNAcylation nuclear pore complex protein stability ubiquitination nucleoporin glycosylation

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Regulation of FLC nuclear import by coordinated action of the NUP62-subcomplex and importinβSAD2

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Journal of Integrative Plant Biology 2023年第9期65卷 2086-2106页

作者： Gang Chen Danyun Xu Qing Liu Zhichuang Yue Biao Dai Shujuan Pan Yongqiang Chen Xinhua Feng Honghong Hu National Key Laboratory of Crop Genetic Improvement Hubei Hongshan LaboratoryHuazhong Agricultural UniversityWuhan 430070China

Flowering locus C(FLC)is a central transcriptional repressor that controls flowering ***,how FLC is imported into the nucleus is ***,we report that Arabidopsis nucleoporins 62(NUP62),NUP58,and NUP54 composed NUP62-subcomplex modulates FLC nuclear import during floral transition in an importinα-independent manner,via direct ***62 recruits FLC to the cytoplasmic filaments and imports it into the nucleus through the NUP62-subcomplex composed central ***βsupersensitive to ABA and drought 2(SAD2),a carrier protein,is critical for FLC nuclear import and flower transition,which facilitates FLC import into the nucleus mainly through the ***,RNAseq,and cell biological analyses indicate that the NUP62-subcomplex mainly mediates the nuclear import of cargos with unconventional nuclear localization sequences(NLSs),such as *** findings illustrate the mechanisms of the NUP62-subcomplex and SAD2 on FLC nuclear import process and floral transition,and provide insights into the role of NUP62-subcomplex and SAD2 in protein nucleocytoplasmic transport in plants.

关键词： FLC flowering time importin nuclear import nucleoporin

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Deguelin regulates nuclear pore complex proteins Nup98 and Nup88 in U937 cells in vitro1

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Acta Pharmacologica Sinica 2005年第10期26卷 1265-1273页

作者： Hong-li LIU~2, Yan CHEN~(2,3), Guo-hui CUI~2, Qiu-ling WU~2, Jing HE~2, Wei-hua CHEN~2, Jian-feng ZHOU~4 ~2 Department of Hematology, Union Hospital, Tongji Medical College, Huazhong University of Science and Technology, Wuhan 430022 ~4 Department of Hematology, Tongji Hospital, Tongji Medical College, Huazhong University of Science and Technology, Wuhan 430030, China Department of Hematology Union Hospital Tongji Medical College Huazhong University of Science and Technology Wuhan 430022

Aim: To investigate the anticancer effects and the molecular mechanisms of deguelin on human U937 leukemia cells, and to explore the underlying mechanism regulating nucleoporin 98 （Nup98） and nucleoporin 88 （Nup88） in vitro. Methods: The effects of deguelin on the growth of U937 cells were studied by MTT assay. The effect of deguelin on the cell cycle of U937 cells was studied by using a propidium iodide method. The localization of the nuclear pore complex proteins Nup98 and Nup88 was investigated by using immunofluorescence and immunoelectron microscopy. The expression of Nup98 and Nup88 in U937 cells was investigated by using flow cytometry and Western blot. Results: The prolif eration of U937 cells was inhibited in the deguelin-treated group, with a 24-h IC50value of 21.61 nmol/L and a 36-h IC50value of 17.07 nmol/L. U937 cells treated with deguelin had reduced percentages of cells in the G0/G1phase, whereas cells accumulated in the S and G2/M phases. Nup88 and Nup98 were found on both the nuclar and cytoplasmic sides of the U937 cells by using immunofluorescence and immunoelectron microscopy. The expression of Nup98 was upregulated and that of the Nup88 protein was downregulated in U937 cells treated with deguelin. Conclusion: Deguelin is able to inhibit the proliferation of U937 cells by regulating the cell cycle such that cells are arrested at the S and G2/M phases, so that the proportion of cells in the G0/G1phase decreases. The antitumor effects of deguelin are related to upregulating the expression of Nup98 and downregulating the expression of Nup88 protein in U937 cells.

关键词： deguelin U937 cells nucleoporin Nup98 Nup88

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