FCH/Cdc15 domain determines distinct subcellular localization of NOSTRIN

被引：18

作者：

Icking, A ^{[1
]}

Schilling, K ^{[1
]}

Wiesenthal, A ^{[1
]}

Opitz, N ^{[1
]}

Müller-Esterl, W ^{[1
]}

机构：

[1] Univ Frankfurt, Inst Biochem 2, Sch Med, D-60590 Frankfurt, Germany

来源：

FEBS LETTERS | 2006年 / 580卷 / 01期

关键词：

NOSTRIN; NO synthase; nitric oxide; FCH; Cdc15;

D O I：

10.1016/j.febslet.2005.11.078

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

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.

引用

页码：223 / 228

页数：6

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