板层素与中间丝的相互作用。
Interaction of plectin and intermediate filaments.
机构信息
Department of Dermatology, School of Medicine, and Institute of Cutaneous Cell Biology, Kurume University, 67 Asahimachi, Kurume, Fukuoka, Japan.
出版信息
J Dermatol Sci. 2012 Apr;66(1):44-50. doi: 10.1016/j.jdermsci.2012.01.008. Epub 2012 Jan 24.
BACKGROUND
Plectin, a member of the plakin family proteins, is a high molecular weight protein that is ubiquitously expressed. It acts as a cytolinker for the three major components of the cyotoskeleton, namely actin microfilaments, microtubules and intermediate filaments.
OBJECTIVE
The aim of our experiments was to identify new binding sites for intermediate filaments on plectin and to specify these sites.
METHODS
We introduced truncated forms of plectin into several cell lines and observe interaction between plectin and intermediate filaments.
RESULTS
We found that a linker region in the COOH-terminal end of plectin was required for the association of the protein with intermediate filaments. In addition, we also demonstrated that a serine residue at position 4645 of plectin may have a role on binding of plectin to intermediate filaments.
CONCLUSION
A linker region in the COOH-terminal end and serine residue at position 4645 may be important for the binding of plectin to intermediate filaments.
背景
网蛋白是斑联蛋白家族蛋白的成员，是一种广泛表达的高分子量蛋白。它作为细胞骨架的三种主要成分——肌动蛋白微丝、微管和中间丝的细胞连接蛋白。
目的
我们实验的目的是鉴定网蛋白上中间丝的新结合位点，并对这些位点进行描述。
方法
我们将截短形式的网蛋白引入几种细胞系中，观察网蛋白与中间丝之间的相互作用。
结果
我们发现网蛋白 COOH 末端的连接区对于该蛋白与中间丝的结合是必需的。此外，我们还证明了网蛋白第 4645 位丝氨酸残基可能在网蛋白与中间丝的结合中发挥作用。
结论
COOH 末端的连接区和第 4645 位丝氨酸残基对于网蛋白与中间丝的结合可能很重要。
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