Evans David E, Pawar Vidya, Smith Sarah J, Graumann Katja
Department of Biological and Medical Sciences, Oxford Brookes University Oxford, UK.
Front Plant Sci. 2014 May 7;5:183. doi: 10.3389/fpls.2014.00183. eCollection 2014.
Following the description of SAD1/UNC84 (SUN) domain proteins in higher plants, evidence has rapidly increased that plants contain a functional linker of nucleoskeleton and cytoskeleton (LINC) complex bridging the nuclear envelope (NE). While the SUN domain proteins appear to be highly conserved across kingdoms, other elements of the complex are not and some key components and interactions remain to be identified. This mini review examines components of the LINC complex, including proteins of the SUN domain family and recently identified plant Klarsicht/Anc/Syne-1 homology (KASH) domain proteins. First of these to be described were WIPs (WPP domain interacting proteins), which act as protein anchors in the outer NE. The plant KASH homologs are C-terminally anchored membrane proteins with the extreme C-terminus located in the nuclear periplasm; AtWIPs contain a highly conserved X-VPT motif at the C-terminus in contrast to PPPX in opisthokonts. The role of the LINC complex in organisms with a cell wall, and description of further LINC complex components will be considered, together with other potential plant-specific functions.
随着高等植物中SAD1/UNC84（SUN）结构域蛋白的相关描述出现，越来越多的证据表明植物含有一种连接核骨架与细胞骨架的功能性复合物（LINC），它横跨核膜（NE）。虽然SUN结构域蛋白在不同生物界中似乎高度保守，但该复合物的其他元件并非如此，一些关键组分和相互作用仍有待确定。这篇小型综述研究了LINC复合物的组分，包括SUN结构域家族的蛋白以及最近鉴定出的植物Klarsicht/Anc/Syne-1同源（KASH）结构域蛋白。首先被描述的是WIPs（WPP结构域相互作用蛋白），它们在外核膜中作为蛋白锚定物发挥作用。植物KASH同源物是C端锚定的膜蛋白，其极端C端位于核周质中；与后生动物中的PPPX不同，拟南芥WIPs在C端含有一个高度保守的X-VPT基序。我们将探讨LINC复合物在具有细胞壁的生物体中的作用，以及对LINC复合物其他组分的描述，同时还会涉及其他潜在的植物特异性功能。
