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Membrane-Mediated Cooperativity of Proteins
Annual Review of Physical Chemistry ( IF 11.7 ) Pub Date : 2018-04-20 00:00:00 , DOI: 10.1146/annurev-physchem-052516-050637
Thomas R. Weikl 1
Affiliation  

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.

中文翻译:


膜介导的蛋白质协同作用

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成型和粘附中的装配和协同功能也起着重要作用。生物膜的复杂形状是由局部诱导膜弯曲的蛋白质产生的。这些蛋白质之间会发生间接的曲率介导的相互作用,因为这些蛋白质共同影响了膜的弯曲能。这些曲率介导的相互作用对新月形蛋白质具有吸引力,并且是膜管形成过程中蛋白质组装的驱动力。膜粘附是由锚定在相对膜上的受体和配体蛋白的结合产生的。这些蛋白质的结合强烈取决于膜的纳米级形状波动,导致波动介导的结合合作性。膜粘附区域中受体-配体复合物之间的长度不匹配会导致排斥曲率介导的相互作用,这是膜粘附过程中基于长度的蛋白质分离的驱动力。

更新日期:2018-04-20
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