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首页> 外文期刊>Journal of cellular biochemistry. >NP/NMP4 transcription factors have distinct osteoblast nuclear matrix subdomains.
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NP/NMP4 transcription factors have distinct osteoblast nuclear matrix subdomains.

机译：NP / NMP4转录因子具有独特的成骨细胞核基质亚结构域。

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摘要

The mechanisms underlying the coupling of type I collagen and matrix metalloproteinase (MMP) expression to cell structure and adhesion are poorly understood. We propose that nuclear matrix architectural transcription factors link cell structure and transcription via their association with nuclear matrix subdomains and by their capacity for altering promoter geometry. NP/NMP4 are nuclear matrix proteins that contain from five to eight Cys(2)His(2) zinc fingers. Some NP/NMP4 isoforms bind to the rat type I collagen alpha1(I) polypeptide chain promoter in the manner of architectural transcription factors and alter basal transcription in osteoblast-like cells (Thunyakitpisal et al. in review). Certain isoforms of NP/NMP4 are identical to CIZ, Cas-interacting zinc finger protein, a nucleocytoplasmic shuttling protein that associates with focal adhesions and regulates MMP expression [Nakamoto et al. (2000): Mol Cell Biol 20:1649-1658]. To better understand the role of subnuclear architecture in collagen and MMP expression, we mapped the osteoblast nuclear distribution of NP/NMP4 proteins and identified the functional motifs necessary for nuclear localization and nuclear matrix targeting. Immunofluorescence microscopy was used to determine the cellular and subnuclear distribution of native NP/NMP4 proteins and green fluorescent protein (GFP)-NP/NMP4 fusion proteins in osteoblast-like cells. All GFP-NP/NMP4 fusion proteins localized to the nucleus, but accumulated in distinct nuclear matrix subdomains. The zinc finger domain was necessary and sufficient for nuclear import and matrix targeting. We conclude that the arrangement of the NP/NMP4 zinc fingers largely determines the subnuclear location of these isoforms. Copyright 2000 Wiley-Liss, Inc.
机译：I型胶原蛋白和基质金属蛋白酶（MMP）表达偶联到细胞结构和粘附的潜在机制了解甚少。我们建议核基质建筑转录因子通过与核基质亚结构域的关联以及它们改变启动子几何形状的能力来链接细胞结构和转录。 NP / NMP4是包含五到八个Cys（2）His（2）锌指的核基质蛋白。一些NP / NMP4亚型以建筑转录因子的方式与大鼠I型胶原蛋白alpha1（I）多肽链启动子结合，并改变成骨细胞样细胞中的基础转录（Thunyakitpisal等人，正在复习）。 NP / NMP4的某些同工型与CIZ（与Cas相互作用的锌指蛋白）相同，CIZ是一种与粘着斑相关并调节MMP表达的核质穿梭蛋白[Nakamoto等。 （2000）：Mol Cell Biol 20：1649-1658]。为了更好地了解亚核结构在胶原蛋白和MMP表达中的作用，我们绘制了NP / NMP4蛋白的成骨细胞核分布图，并确定了核定位和核基质靶向所必需的功能性基序。免疫荧光显微镜用于确定成骨样细胞中天然NP / NMP4蛋白和绿色荧光蛋白（GFP）-NP / NMP4融合蛋白的细胞和亚核分布。所有GFP-NP / NMP4融合蛋白都位于细胞核内，但聚集在不同的核基质亚结构域中。锌指结构域对于核输入和基质靶向而言是必要和充分的。我们得出结论，NP / NMP4锌指的排列在很大程度上决定了这些同工型的亚核位置。版权所有2000 Wiley-Liss，Inc.

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