Murine GBP-2: a new IFN-gamma-induced member of the GBP family of GTPases isolated from macrophages.

Murine GBP-2: a new IFN-gamma-induced member of the GBP family of GTPases isolated from macrophages.
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鼠 GBP-2:从巨噬细胞中分离出的 GTP 酶 GBP 家族的新 IFN-γ 诱导成员。

DOI:
10.1089/jir.1998.18.977
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发表时间:
1998
期刊:
Journal of interferon & cytokine research : the official journal of the International Society for Interferon and Cytokine Research.
影响因子:
--
通讯作者:
Maki,RA
Maki,RA
中科院分区:
--
文献类型:
--
作者:
Vestal,DJ;Buss,JE;McKercher,SR;Jenkins,NA;Copeland,NG;Kelner,GS;Asundi,VK;Maki,RA

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我们从骨髓来源的巨噬细胞中克隆了干扰素(IFN)诱导的鸟苷酸结合蛋白(GBP) gtp酶家族的新成员,小鼠GBP-2 (mGBP-2)。mGBP-2位于小鼠3号染色体上,与mGBP-1相连。随着mGBP-2的鉴定,现在有两种人类GBPs和两种小鼠GBPs。与其他GBPs一样,mgbps -2 RNA和蛋白可被IFN-γ诱导。此外,mGBP-2与其他gbp具有重要的结构特征,这些特征将该家族与其他gtp酶区分开来。首先,在其他GTP酶的经典GTP结合区域中发现的三个核苷酸结合序列中,mGBP-2只包含两个。在mGBP-2中发现的第二个氨基酸基序是一个潜在的类异戊二烯修饰的c端位点,称为CaaX序列。通过[3H]甲羟戊酸掺入检测,mGBP-2在COS细胞中表达时被戊烯化,并优先结合C-20类异戊二烯香叶醇。令人惊讶的是,尽管具有功能性CaaX序列,mGBP-2主要是细胞质。GBP蛋白在ifn暴露的细胞中非常丰富,但对其功能知之甚少。IFN-γ处理的C57B1/6小鼠细胞表达mGBP-2,而mGBP-1不表达。因此,mGBP-2的鉴定使得在没有第二个家庭成员的情况下研究GBP功能成为可能。
We have cloned a new member of the interferon (IFN)-induced guanylate-binding protein (GBP) family of GTPases, murine GBP-2 (mGBP-2), from bone marrow-derived macrophages. mGBP-2 is located on murine chromosome 3, where it is linked to mGBP-1. With the identification of mGBP-2 there are now two human and two murine GBPs. Like other GBPs, mGBP-2 RNA and protein are induced by IFN-γ. In addition, mGBP-2 shares with the other GBPs important structural features that distinguish this family from other GTPases. First, mGBP-2 contains only two of the three consensus sequences for nucleotide binding found within the classic GTP binding regions of other GTPases. A second amino acid motif found in mGBP-2 is a potential C-terminal site for isoprenoid modification, called a CaaX sequence. mGBP-2 is prenylated, as detected by [3H]mevalonate incorporation, when expressed in COS cells and preferentially incorporates the C-20 isoprenoid geranylgeraniol. Surprisingly, despite having a functional CaaX sequence, mGBP-2 is primarily cytosolic. GBP proteins are very abundant in IFN-exposed cells, but little is known about their function. mGBP-2 is expressed by IFN-γ-treated cells from C57B1/6 mice, whereas mGBP-1 is not. Thus, the identification of mGBP-2 makes possible the study of GBP function in the absence of a second family member.
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