典型文献
Myosin 1D and the branched actin network control the condensation of p62 bodies
文献摘要：
Biomolecular condensation driven by liquid-liquid phase separation(LLPS)is key to assembly of membraneless organelles in numerous crucial pathways.It is largely unknown how cellular structures or components spatiotemporally regulate LLPS and condensate formation.Here we reveal that cytoskeletal dynamics can control the condensation of p62 bodies comprising the autophagic adaptor p62/SQSTM1 and poly-ubiquitinated cargos.Branched actin networks are associated with p62 bodies and are required for their condensation.Myosin 1D,a branched actin-associated motor protein,drives coalescence of small nanoscale p62 bodies into large micron-scale condensates along the branched actin network.Impairment of actin cytoskeletal networks compromises the condensation of p62 bodies and retards substrate degradation by autophagy in both cellular models and Myosin 1D knockout mice.Coupling of LLPS scaffold to cytoskeleton systems may represent a general mechanism by which cells exert spatiotemporal control over phase condensation processes.
文献关键词：
中图分类号：
作者姓名：
Xuezhao Feng;Wanqing Du;Mingrui Ding;Wenkang Zhao;Xirenayi Xirefu;Meisheng Ma;Yuhui Zhuang;Xiaoyu Fu;Jiangfeng Shen;Jinpei Zhang;Xiuying Lei;Daxiao Sun;Qing Xi;Yiliyasi Aisa;Qian Chen;Ying Li;Wenjuan Wang;Shanjin Huang;Li Yu;Pilong Li;Na Mi
作者机构：
State Key Laboratory of Pathogenesis,Prevention and Treatment of Central Asian High Incidence Diseases,Clinical Medical Research Institute,The First Affiliated Hospital of Xinjiang Medical University,Urumqi,Xinjiang,China;Basic Medical College,Xinjiang Medical University,Urumqi,Xinjiang,China;State Key Laboratory of Membrane Biology,Tsinghua University-Peking University Joint Center for Life Sciences,School of Life Sciences,Tsinghua University,Beijing,China;Beijing Advanced Innovation Center for Structural Biology & Frontier Research Center for Biological Structure,Tsinghua University-Peking University Joint Center for Life Sciences,School of Life Sciences,Tsinghua University,Beijing,China;College of Pharmacy,Xinjiang Medical University,Urumqi,Xinjiang,China;Tongji Medical College of Huazhong University of Science and Technology,Wuhan,Hubei,China;Center for Plant Biology,School of Life Sciences,Tsinghua University,Beijing,China;Ministry of Education Key Laboratory of Protein Sciences,Beijing Advanced Innovation Center for Structural Biology,Beijing Frontier Research Center of Biological Structures,School of Life Sciences,Tsinghua University,Beijing,China;Center of Biomedical Analysis,Tsinghua University,Beijing,China
文献出处：
引用格式：
[1]Xuezhao Feng;Wanqing Du;Mingrui Ding;Wenkang Zhao;Xirenayi Xirefu;Meisheng Ma;Yuhui Zhuang;Xiaoyu Fu;Jiangfeng Shen;Jinpei Zhang;Xiuying Lei;Daxiao Sun;Qing Xi;Yiliyasi Aisa;Qian Chen;Ying Li;Wenjuan Wang;Shanjin Huang;Li Yu;Pilong Li;Na Mi-.Myosin 1D and the branched actin network control the condensation of p62 bodies)[J].细胞研究（英文版）,2022(07):659-669
A类：
membraneless
B类：
Myosin,1D,branched,actin,control,condensation,p62,bodies,Biomolecular,driven,by,liquid,phase,separation,LLPS,key,assembly,organelles,numerous,crucial,pathways,It,largely,unknown,how,cellular,structures,components,spatiotemporally,regulate,formation,Here,we,reveal,that,cytoskeletal,dynamics,can,comprising,autophagic,adaptor,SQSTM1,poly,ubiquitinated,cargos,Branched,networks,are,associated,required,their,motor,protein,drives,coalescence,small,nanoscale,into,micron,condensates,along,Impairment,compromises,retards,substrate,degradation,autophagy,both,models,knockout,mice,Coupling,scaffold,cytoskeleton,systems,may,represent,general,mechanism,which,cells,exert,over,processes
AB值：
0.603186
相似文献
机标中图分类号，由域田数据科技根据网络公开资料自动分析生成，仅供学习研究参考。
