Ciz, a transcription factor with a nucleocytoplasmic shuttling activity, interacts with C-propeptides of type I collagen
Ciz, a transcription factor with a nucleocytoplasmic shuttling activity, interacts with C-propeptides of type I collagen
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DOI：
10.1016/j.bbrc.2008.01.040
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发表时间：
2008-04-04
影响因子：
3.1
通讯作者：
Noda, Masaki
中科院分区：
文献类型：
--
作者：
Hayata, Tadayoshi;Nakamoto, Tetsuya;Noda, Masaki
CIZ是一种具有核质穿梭活性的锌指转录因子。CIZ基因缺陷小鼠表现为高骨量表型。作为解决CIZ如何抑制骨形成的第一步，我们基于酵母双杂交筛选检查了CIZ的结合伙伴。虽然CIZ是细胞内蛋白，但47%的阳性克隆是编码细胞外基质蛋白的基因，包括Colla1、Colla2、FbIn2和rpsA。用体外翻译的蛋白质进行的体外免疫共沉淀实验表明，CIZ-Delta ZF(锌指)直接与和Colla2的C-前肽结合。用免疫沉淀法在COS-7细胞中观察到CIZ基因与Colla1 C-前肽的体内结合。在细胞内定位方面，COIL和CIZ高表达的C-原肽共定位于细胞核。这些结果表明，CIZ与I型胶原的C-前肽相互作用，这种相互作用发生在细胞核内。(C)2008 Elsevier Inc.保留所有权利。
Ciz is a zinc finger transcription factor with nucleocytoplasmic shuttling activity. Ciz-deficient mice show high bone mass phenotype. As a first step to address how Ciz suppresses bone formation, we examined the binding partners of Ciz based on a yeast two-hybrid screening. While Ciz is an intracellular protein, 47% of the positive clones were genes encoding extracellular matrix proteins, including Colla1, Colla2, FbIn2, and Rpsa. In vitro coimmunoprecipitation experiments using in vitro translated proteins revealed direct binding of Ciz-Delta ZF (zinc finger) to C-propeptides of and Colla2. In vivo association of the transfected Ciz and C-propeptide of Colla1 was observed in COS-7 cells based on immunoprecipitation. In terms of intracellular localization, overexpressed C-propeptides of Coll and Ciz were co-localized in nuclei. These results revealed that Ciz interacts with C-propeptides of type I collagen and this association takes place in nuclei. (C) 2008 Elsevier Inc. All rights reserved.