Protein prenylation and synaptic plasticity: implications for Alzheimer's disease.
Protein prenylation and synaptic plasticity: implications for Alzheimer's disease.
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DOI：
10.1007/s12035-013-8627-z
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发表时间：
2014-08
影响因子：
5.1
通讯作者：
Li, Ling
中科院分区：
文献类型：
--
作者：
Hottman, David A.;Li, Ling
关键词：
蛋白质异戊烯化是一种重要的蛋白质脂质翻译后修饰。它包括蛋白质法尼基化和香叶基香叶基化，其中15-碳法尼基焦磷酸或20-碳香叶基香叶基焦磷酸分别被法尼基转移酶或香叶基香叶基转移酶催化连接到靶蛋白的C-末端。蛋白质异戊二烯化促进蛋白质锚定到细胞膜中并介导蛋白质-蛋白质相互作用。在许多经历异戊烯化的蛋白质中，小GTP酶代表了最大的异戊烯化蛋白质组。小GTP酶参与调节包括突触可塑性在内的多种细胞功能。小GTP酶的异戊烯化状态决定了蛋白质的亚细胞位置和功能。小GTP酶的失调或功能障碍导致不同类型的疾病的发展。新出现的证据表明，异戊二烯化蛋白，特别是小GTP酶，可能在阿尔茨海默病的发病机制中发挥重要作用。本文综述了小GTP酶Ras和Rho亚家族的异戊烯化及其与突触可塑性和阿尔茨海默病的关系。
Protein prenylation is an important lipid posttranslational modification of proteins. It includes protein farnesylation and geranylgeranylation, in which the 15-carbon farnesyl pyrophosphate or 20-carbon geranylgeranyl pyrophosphate is attached to the C-terminus of target proteins, catalyzed by farnesyl transferase or geranylgeranyl transferases, respectively. Protein prenylation facilitates the anchoring of proteins into the cell membrane and mediates protein-protein interactions. Among numerous proteins that undergo prenylation, small GTPases represent the largest group of prenylated proteins. Small GTPases are involved in regulating a plethora of cellular functions including synaptic plasticity. The prenylation status of small GTPases determines the subcellular locations and functions of the proteins. Dysregulation or dysfunction of small GTPases leads to the development of different types of disorders. Emerging evidence indicates that prenylated proteins, in particular small GTPases, may play important roles in the pathogenesis of Alzheimer’s disease. This review focuses on the prenylation of Ras and Rho subfamilies of small GTPases and its relation to synaptic plasticity and Alzheimer’s disease.
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