Molecular insights into LINC complex architecture through the crystal structure of a luminal trimeric coiled-coil domain of SUN1.
Molecular insights into LINC complex architecture through the crystal structure of a luminal trimeric coiled-coil domain of SUN1.
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DOI：
10.3389/fcell.2023.1144277
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发表时间：
2023
影响因子：
5.5
通讯作者：
中科院分区：
文献类型：
--
作者：
LINC复合物由相互作用的SUN和KASH蛋白组成，机械地将核内容物偶联到细胞骨架上。在减数分裂中，LINC复合体将微管产生的力传递到染色体末端，驱动染色体的快速运动，这是突触和交叉所必需的。在体细胞中，它定义了细胞核的形状和位置，并有许多特殊的作用，包括听觉。在这里，我们报道了SUN1的管腔区域的一个卷曲结构域的x射线晶体结构，为SUN1如何穿过核管腔，从内层核膜到与外核膜上的KASH蛋白相互作用提供了一个架构基础。结合光和x射线散射，分子动力学和结构定向建模，我们提出了一个太阳1的整个光腔区域的模型。该模型强调了结构域之间固有的灵活性，并提出了结构域交换相互作用可能建立LINC复杂网络以协调细胞骨架力传递的可能性。
The LINC complex, consisting of interacting SUN and KASH proteins, mechanically couples nuclear contents to the cytoskeleton. In meiosis, the LINC complex transmits microtubule-generated forces to chromosome ends, driving the rapid chromosome movements that are necessary for synapsis and crossing over. In somatic cells, it defines nuclear shape and positioning, and has a number of specialised roles, including hearing. Here, we report the X-ray crystal structure of a coiled-coiled domain of SUN1’s luminal region, providing an architectural foundation for how SUN1 traverses the nuclear lumen, from the inner nuclear membrane to its interaction with KASH proteins at the outer nuclear membrane. In combination with light and X-ray scattering, molecular dynamics and structure-directed modelling, we present a model of SUN1’s entire luminal region. This model highlights inherent flexibility between structured domains, and raises the possibility that domain-swap interactions may establish a LINC complex network for the coordinated transmission of cytoskeletal forces.
影响因子：
5.7
作者：
Lim, Sing Mei;Cruz, Victor E.;Antoku, Susumu;Gundersen, Gregg G.;Schwartz, Thomas U.
通讯作者：
Schwartz, Thomas U.