FCH/Cdc15 domain determines distinct subcellular localization of NOSTRIN
FCH/Cdc15 domain determines distinct subcellular localization of NOSTRIN
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DOI：
10.1016/j.febslet.2005.11.078
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发表时间：
2006-01-09
期刊：
影响因子：
3.5
通讯作者：
M端ller-Esterl, W
中科院分区：
文献类型：
--
作者：
Icking, A;Schilling, K;M端ller-Esterl, W
NOSTRIN是一种非合成酶结合蛋白，属于PCH蛋白家族，具有典型的结构域结构。虽然它的SH3结构域和C-末端螺旋圈区CC2已经被研究过了，但N-末端的一半由带有FCH(Fes/CIP Homology)区的CDC15结构域和紧随其后的螺旋线圈拉伸鳗鱼组成，其功能尚不清楚。在这里，我们证明了FCH区域是NOSTRIN膜结合的必要条件和充分条件，而CDC15区域进一步指定了蛋白质的亚细胞分布。因此，FCH区和CDC15结构域在NOSTRIN的亚细胞靶向中实现互补功能。(C)2005年欧洲生化学会联合会。爱思唯尔出版，版权所有。
NOSTRIN, an NO synthase binding protein, belongs to the PCH family of proteins, exposing a typical domain structure. While its SH3 domain and the C-terminal coiled-coil region cc2 have been studied earlier, the function of the N-terminal half comprising a Cdc15 domain with an FCH (Fes/CIP homology) region followed by a coiled-coil stretch eel is unknown. Here, we show that the FCH region is necessary and sufficient for membrane association of NOSTRIN, whereas the Cdc15 domain further specifies subcellular distribution of the protein. Thus, the FCH region and the Cdc15 domain fulfill complementary functions in subcellular targeting of NOSTRIN. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.