BERP, a novel ring finger protein, binds to α-actinin-4
BERP, a novel ring finger protein, binds to α-actinin-4
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DOI：
10.1006/bbrc.1999.2045
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发表时间：
2000-01-27
影响因子：
3.1
通讯作者：
Vincent, SR
中科院分区：
文献类型：
--
作者：
El-Husseini, AED;Kwasnicka, D;Vincent, SR
我最近鉴定出BERP是一种新的RING指蛋白，属于RBCC蛋白家族。它含有N-末端RING指，随后是B-盒锌指和卷曲螺旋结构域。BERP通过BERP C-末端中的β-螺旋桨结构与V类肌球蛋白的尾部结构域相互作用。为了鉴定与BERP相互作用的其他蛋白质，采用S-east双杂交策略，使用RBCC结构域作为诱饵。筛选大鼠脑cDNA文库，鉴定α-辅肌动蛋白-4为BERP N-末端的特异性结合伴侣。这种辅肌动蛋白同种型可以与来自用BERP和α-辅肌动蛋白-4的表达构建体转染的HEK 293细胞的BERP一起免疫沉淀。这些蛋白质也可以化学共定位在分化的PC 12细胞的细胞质中。我们认为BERP可能通过与α-辅肌动蛋白-4相互作用将V类肌球蛋白锚到特定的细胞结构域。(C)北京大学出版社.
me recently identified BERP as a novel RING finger protein belonging to the RBCC protein family. it contains an N-terminal RING finger, followed by a B-box zinc finger and a coiled-coil domain. BERP interacts with the tail domain of the class V myosins through a beta-propeller structure in the BERP C-terminal. To identify other proteins interacting with BERP, the S-east two-hybrid strategy was employed, using the RBCC domain as bait. Screening of a rat brain cDNA library identified alpha-actinin-4 as a specific binding partner for the N-terminus of BERP. This actinin isoform could be immunoprecipitated together with BERP from HEK 293 cells transfected with expression constructs for BERP and alpha-actinin-4. These proteins could also be colocalized immunohistochemically in the cytoplasm of differentiated PC12 cells. We suggest that BERP may anchor class V myosins to particular cell domains Via its interaction with alpha-actinin-4. (C) 2000 Academic Press.