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首页> 外文期刊>Molecular and Cellular Biology >Spatial Distribution and Function of Sterol Regulatory Element-Binding Protein 1a and 2 Homo- and Heterodimers by In Vivo Two-Photon Imaging and Spectroscopy Fluorescence Resonance Energy Transfer
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Spatial Distribution and Function of Sterol Regulatory Element-Binding Protein 1a and 2 Homo- and Heterodimers by In Vivo Two-Photon Imaging and Spectroscopy Fluorescence Resonance Energy Transfer

机译：体内双光子成像和光谱荧光共振能量转移的甾醇调节元件结合蛋白1a和2同-和异二聚体的空间分布和功能。

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Sterol regulatory element-binding proteins (SREBPs) are a subfamily of basic helix-loop-helix-leucine zipper proteins that regulate lipid metabolism. We show novel evidence of the in vivo occurrence and subnuclear spatial localization of both exogenously expressed SREBP-1a and -2 homodimers and heterodimers obtained by two-photon imaging and spectroscopy fluorescence resonance energy transfer. SREBP-1a homodimers localize diffusely in the nucleus, whereas SREBP-2 homodimers and the SREBP-1a/SREBP-2 heterodimer localize predominantly to nuclear speckles or foci, with some cells showing a diffuse pattern. We also used tethered SREBP dimers to demonstrate that both homo- and heterodimeric SREBPs activate transcription in vivo. Ultrastructural analysis revealed that the punctate foci containing SREBP-2 are electron-dense nuclear bodies, similar or identical to structures containing the promyelocyte (PML) protein. Immunofluorescence studies suggest that a dynamic interplay exists between PML, as well as another component of the PML-containing nuclear body, SUMO-1, and SREBP-2 within these nuclear structures. These findings provide new insight into the overall process of transcriptional activation mediated by the SREBP family.
机译：甾醇调节元件结合蛋白（SREBPs）是调节脂质代谢的基本螺旋-环-螺旋-亮氨酸拉链蛋白的一个亚家族。我们显示了新出现的证据，通过双光子成像和光谱荧光共振能量转移获得的外源表达的SREBP-1a和-2同二聚体和异二聚体的体内发生和亚核空间定位。 SREBP-1a同型二聚体分散在细胞核中，而SREBP-2同型二聚体和SREBP-1a / SREBP-2异二聚体主要分布在核斑点或病灶上，有些细胞呈散布型。我们还使用拴系的SREBP二聚体来证明同二聚体和异二聚体SREBPs在体内均能激活转录。超微结构分析表明，含有SREBP-2的点状灶是电子致密核体，与含有早幼粒细胞（PML）蛋白的结构相似或相同。免疫荧光研究表明，PML之间以及这些核结构中包含PML的核体SUMO-1和SREBP-2的另一个组成部分之间存在动态相互作用。这些发现为SREBP家族介导的转录激活的整个过程提供了新的见识。

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