Herpes simplex virus type 2 membrane protein UL56 associates with the kinesin motor protein KIF1A
Herpes simplex virus type 2 membrane protein UL56 associates with the kinesin motor protein KIF1A
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DOI：
10.1099/vir.0.80633-0
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发表时间：
2005-03-01
影响因子：
3.8
通讯作者：
Nishiyama, Y
中科院分区：
文献类型：
--
作者：
Koshizuka, T;Kawaguchi, Y;Nishiyama, Y
单纯疱疹病毒UL56基因产物是一种C末端锚定的11型膜蛋白，功能未知。在酵母双杂交筛选和GST下拉实验中，UL56被发现与Kinesin-3家族的成员KIF1A相互作用。KIF1A介导突触小泡前体的运输，对神经元的功能和活性是必不可少的。当过表达时，KIF1 A与全长UL56共定位，但当与缺少C末端跨膜区的UL56突变蛋白共表达时，没有观察到明显的共定位。虽然在酵母双杂交筛选和GST下拉实验中，C端TMD对与KIF1 A的相互作用不是必需的，但这些结果表明UL56的C端TMD以及AA69-217对于体内与KIF1 A的相互作用是重要的。讨论了UL56蛋白可能通过作为神经元中运动蛋白的受体来影响感染细胞中的囊泡运输的假说。
The herpes simplex virus UL56 gene product is a C-terminal-anchored, type 11 membrane protein of unknown function. UL56 was found to interact with KIF1 A, a member of the kinesin-3 family, in a yeast two-hybrid screen and a GST pull-down assay. KIF1 A mediates the transport of synaptic vesicle precursors and is essential for the function and viability of neurons. When overexpressed, KIF1 A co-localized with full-sized UL56, but no clear co-localization was observed when co-expressed with the UL56 mutant protein lacking its C-terminal transmembrane domain - (TIMID). Although the C-terminal TMD was not essential for the interaction with KIF1 A in the yeast two-hybrid screen and GST pull-down assays, these results indicate that the C-terminal TMD, as well as aa 69-217, of UL56 are important for the interaction with KIF1 A in vivo. The hypothesis that the UL56 protein affects vesicular trafficking in infected cells, potentially by acting as a receptor for motor proteins in neurons, is discussed.