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作 者:Xue-Ni Hou Chun Tang
机构地区:[1]Beijing National Laboratory for Molecular Sciences,College of Chemistry and Molecular Engineering,Peking University,Beijing 100871,China,and [2]Center for Quantitate Biology,PKU-Tsinghua Center for Life Science,Academy for Advanced Interdisciplinary Studies,Peking University,Beijing 100871,China
出 处:《Acta Biochimica et Biophysica Sinica》2023年第7期1084-1098,共15页生物化学与生物物理学报(英文版)
基 金:supported by the grant from the National Key R&D Program of China(No.2018YFA0507700).
摘 要:Ubiquitination,a post-translational modification that attaches one or more ubiquitin(Ub)molecules to another protein,plays a crucial role in the phase-separation processes.Ubiquitination can modulate the formation of membrane-less organelles in two ways.First,a scaffold protein drives phase separation,and Ub is recruited to the condensates.Second,Ub actively phase-separates through the interactions with other proteins.Thus,the role of ubiquitination and the resulting polyUb chains ranges from bystanders to active participants in phase separation.Moreover,long polyUb chains may be the primary driving force for phase separation.We further discuss that the different roles can be determined by the lengths and linkages of polyUb chains which provide preorganized and multivalent binding platforms for other client proteins.Together,ubiquitination adds a new layer of regulation for the flow of material and information upon cellular compartmentalization of proteins.
关 键 词:UBIQUITINATION phase separation stress granule polyubiquitin chain post-translational modification
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