Septin Interferes with the Temperature-Dependent Domain Formation and Disappearance of Lipid Bilayer Membranes.
Septin Interferes with the Temperature-Dependent Domain Formation and Disappearance of Lipid Bilayer Membranes.
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Septin 干扰脂质双层膜的温度依赖性域的形成和消失。
DOI：
10.1021/acs.langmuir.6b03452
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发表时间：
2016
期刊：
影响因子：
--
通讯作者：
K. Takiguchi
中科院分区：
文献类型：
--
作者：
Shunsuke Yamada;Takumi Isogai;R. Tero;Y. Tanaka;T. Ujihara;M. Kinoshita;K. Takiguchi
脂质双层膜中的结构域形成或区室化被认为是在细胞膜中动态发生的，并且在其生理功能的时空调节中起重要作用。此外，作为细胞膜下的蛋白质组装体的膜骨架也调节膜的性质以及形态，因为其作为膜的组成分子的扩散屏障或作为生理反应的支架的作用。因此，研究脂质双层膜与构成膜骨架的蛋白质之间的关系具有重要意义。在细胞骨架系统中，septin是独特的，因为它在含有磷酸肌醇的脂质体上形成阵列，并且这种性质被认为有助于精子鞭毛中环带的形成。在这项研究中，支持的脂质双层（SLB）被用来调查的影响，septin对脂质双层，因为SLB，而不是脂质体是适合于观察形成的膜域。我们发现，SLB含有磷脂酰肌醇（PI）可逆地形成域通过降低温度和septin影响的冷却诱导域的形成和消失。Septin在温度降低期间抑制冷却诱导域的生长，并且在温度升高期间抑制这些域的分散和消失。这些结果表明Septin复合物，即，聚集在脂质双层膜表面的细丝或寡聚体，可以通过它们作为PI分子的锚的行为来调节结构域形成的动力学。
Domain formation or compartmentalization in a lipid bilayer membrane has been thought to take place dynamically in cell membranes and play important roles in the spatiotemporal regulation of their physiological functions. In addition, the membrane skeleton, which is a protein assembly beneath the cell membrane, also regulates the properties as well as the morphology of membranes because of its role as a diffusion barrier against constitutive molecules of the membrane or as a scaffold for physiological reactions. Therefore, it is important to study the relationship between lipid bilayer membranes and proteins that form the membrane skeleton. Among cytoskeletal systems, septin is unique because it forms arrays on liposomes that contain phosphoinositides, and this property is thought to contribute to the formation of the annulus in sperm flagellum. In this study, a supported lipid bilayer (SLB) was used to investigate the effect of septin on lipid bilayers because SLBs rather than liposomes are suitable for observation of the membrane domains formed. We found that SLBs containing phosphatidylinositol (PI) reversibly form domains by decreasing the temperature and that septin affects both the formation and the disappearance of the cooling-induced domain. Septin inhibits the growth of cooling-induced domains during decreases in temperature and inhibits the dispersion and the disappearance of those domains during increases in temperature. These results indicate that septin complexes, i.e., filaments or oligomers assembling on the surface of lipid bilayer membranes, can regulate the dynamics of domain formation via their behavior as an anchor for PI molecules.
影响因子：
5.6
作者：
Bertin A;McMurray MA;Thai L;Garcia G 3rd;Votin V;Grob P;Allyn T;Thorner J;Nogales E
通讯作者：
Nogales E
影响因子：
64.8
作者：
van den Bogaart, Geert;Meyenberg, Karsten;Risselada, H. Jelger;Amin, Hayder;Willig, Katrin I.;Hubrich, Barbara E.;Dier, Markus;Hell, Stefan W.;Grubmueller, Helmut;Diederichsen, Ulf;Jahn, Reinhard
通讯作者：
Jahn, Reinhard
影响因子：
11.8
作者：
Kinoshita, M;Field, CM;Mitchison, TJ
通讯作者：
Mitchison, TJ