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蛋白质的膜介导协同作用。

Membrane-Mediated Cooperativity of Proteins.

作者信息

Weikl Thomas R

机构信息

Department of Theory and Bio-Systems, Max Planck Institute of Colloids and Interfaces, 14424 Potsdam, Germany; email:

出版信息

Annu Rev Phys Chem. 2018 Apr 20;69:521-539. doi: 10.1146/annurev-physchem-052516-050637. Epub 2018 Feb 28.

Abstract

Besides direct protein-protein interactions, indirect interactions mediated by membranes play an important role for the assembly and cooperative function of proteins in membrane shaping and adhesion. The intricate shapes of biological membranes are generated by proteins that locally induce membrane curvature. Indirect curvature-mediated interactions between these proteins arise because the proteins jointly affect the bending energy of the membranes. These curvature-mediated interactions are attractive for crescent-shaped proteins and are a driving force in the assembly of the proteins during membrane tubulation. Membrane adhesion results from the binding of receptor and ligand proteins that are anchored in the apposing membranes. The binding of these proteins strongly depends on nanoscale shape fluctuations of the membranes, leading to a fluctuation-mediated binding cooperativity. A length mismatch between receptor-ligand complexes in membrane adhesion zones causes repulsive curvature-mediated interactions that are a driving force for the length-based segregation of proteins during membrane adhesion.

摘要

除了直接的蛋白质-蛋白质相互作用外,由膜介导的间接相互作用对于蛋白质在膜塑形和黏附中的组装及协同功能起着重要作用。生物膜的复杂形状是由局部诱导膜曲率的蛋白质产生的。这些蛋白质之间的间接曲率介导相互作用的出现是因为这些蛋白质共同影响膜的弯曲能。这些曲率介导的相互作用对新月形蛋白质具有吸引力,并且是膜微管形成过程中蛋白质组装的驱动力。膜黏附是由锚定在相对膜中的受体和配体蛋白质的结合引起的。这些蛋白质的结合强烈依赖于膜的纳米级形状波动,导致波动介导的结合协同性。膜黏附区域中受体-配体复合物之间的长度不匹配会导致排斥性曲率介导的相互作用,这是膜黏附过程中基于长度的蛋白质分离的驱动力。

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