Structural and functional evaluation of C. elegans filamins FLN-1 and FLN-2.
Structural and functional evaluation of C. elegans filamins FLN-1 and FLN-2.
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DOI：
10.1371/journal.pone.0022428
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发表时间：
2011
期刊：
影响因子：
3.7
通讯作者：
Cram EJ
中科院分区：
文献类型：
--
作者：
DeMaso CR;Kovacevic I;Uzun A;Cram EJ
丝状蛋白是由N-末端肌动蛋白结合结构域（ABD）和多个免疫球蛋白样重复序列（IgFLN）组成的长而灵活的多结构域蛋白。它们的功能是组织和维持肌动蛋白细胞骨架，为信号组分提供支架，并充当机械力传感器。在这项研究中，我们使用转录测序和同源性建模来表征C。线虫细丝蛋白直系同源物FLN-1和FLN-2。结果表明，C.秀丽线虫FLN-1在序列水平上相对于脊椎动物丝状体非常保守，特别是在ABD和几个关键的IgFLN重复序列中。FLN-1和更趋异的FLN-2在体内与肌动蛋白共定位。FLN-2保守性差，至少有23个IgFLN重复序列被似乎是线虫特异性的大区域中断。我们的研究结果表明，许多脊椎动物丝状体的关键特征在C。elegans FLN-1和FLN-2的功能，提示线虫可能是进一步研究细丝蛋白功能的一个非常有用的模型系统。
Filamins are long, flexible, multi-domain proteins composed of an N-terminal actin-binding domain (ABD) followed by multiple immunoglobulin-like repeats (IgFLN). They function to organize and maintain the actin cytoskeleton, to provide scaffolds for signaling components, and to act as mechanical force sensors. In this study, we used transcript sequencing and homology modeling to characterize the gene and protein structures of the C. elegans filamin orthologs fln-1 and fln-2. Our results reveal that C. elegans FLN-1 is well conserved at the sequence level to vertebrate filamins, particularly in the ABD and several key IgFLN repeats. Both FLN-1 and the more divergent FLN-2 colocalize with actin in vivo. FLN-2 is poorly conserved, with at least 23 IgFLN repeats interrupted by large regions that appear to be nematode-specific. Our results indicate that many of the key features of vertebrate filamins are preserved in C. elegans FLN-1 and FLN-2, and suggest the nematode may be a very useful model system for further study of filamin function.
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