In vivo roles of the basic domain of dynactin p150 in microtubule plus-end tracking and dynein function.
In vivo roles of the basic domain of dynactin p150 in microtubule plus-end tracking and dynein function.
复制标题
动力蛋白 p150 基本结构域在微管正端追踪和动力蛋白功能中的体内作用。
DOI：
10.1111/j.1600-0854.2011.01312.x
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发表时间：
2012
期刊：
影响因子：
--
通讯作者：
Xiang,Xin
中科院分区：
文献类型：
--
作者：
Yao,Xuanli;Zhang,Jun;Zhou,Henry;Wang,Eric;Xiang,Xin
微管(MT) +末端跟踪蛋白在MT +末端积累，用于各种细胞功能，但其靶向机制尚不完全清楚（Akhmanova A和Steinmetz MO）。跟踪末端：动态蛋白质网络控制微管尖端的命运。中华生物医学工程学报，2008;9(2):391 - 391。在这里，我们测试了丝状真菌细细曲霉对动力蛋白p150的正端定位的要求，动力蛋白p150是动力蛋白功能所必需的蛋白质。p150 N端MT结合区的缺失显著减少了动力蛋白重链和p150的MT正端积累，并导致核分布的部分缺陷。令人惊讶的是，在MT结合区域内，基本结构域比CAP - Gly（细胞骨架相关蛋白甘氨酸富）结构域更重要，可以维持p150的正端跟踪，以及动力蛋白在核分布和早期内体运动中的功能。我们的结果表明，a的基本定义域。nidulansp150对于体内和体外的p150 - mt相互作用很重要，该结构域内的碱性氨基酸对于野生型背景下p150的正端积累和ΔkinA（kinein - 1）背景下p150 - mt相互作用至关重要。我们认为p150和MTs之间的静电相互作用需要碱性氨基酸，这对于动力蛋白1介导的动力蛋白和动力蛋白inA的正端靶向是重要的。nidulans。
Microtubule (MT) plus‐end‐tracking proteins accumulate at MT plus ends for various cellular functions, but their targeting mechanisms are not fully understood (Akhmanova A and Steinmetz MO. Tracking the ends: a dynamic protein network controls the fate of microtubule tips. Nat Rev Mol Cell Biol 2008;9:309–322.). Here, we tested in the filamentous fungusAspergillus nidulansthe requirement for plus‐end localization of dynactin p150, a protein essential for dynein function. Deletion of the N‐terminal MT‐binding region of p150 significantly diminishes the MT plus‐end accumulation of both dynein heavy chain and p150, and causes a partial defect in nuclear distribution. Surprisingly, within the MT‐binding region, the basic domain is more critical than the CAP‐Gly (cytoskeleton‐associated protein glycine‐rich) domain for maintaining plus‐end tracking of p150, as well as for the functions of dynein in nuclear distribution and early endosome movement. Our results show that the basic domain ofA. nidulansp150 is important for p150–MT interaction bothin vivoandin vitro, and the basic amino acids within this domain are crucial for the plus‐end accumulation of p150 in the wild‐type background and for the p150–MT interaction in the ΔkinA(kinesin‐1) background. We suggest that the basic amino acids are required for the electrostatic interaction between p150 and MTs, which is important for kinesin‐1‐mediated plus‐end targeting of dynactin and dynein inA. nidulans.