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首页> 美国卫生研究院文献>Molecular and Cellular Biology >Visualization of Myc/Max/Mad Family Dimers and the Competition for Dimerization in Living Cells
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Visualization of Myc/Max/Mad Family Dimers and the Competition for Dimerization in Living Cells

机译：Myc / Max / Mad家庭二聚体的可视化和活细胞中二聚化的竞争

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Myc and Mad family proteins play opposing roles in the control of cell growth and proliferation. We have visualized the subcellular locations of complexes formed by Myc/Max/Mad family proteins using bimolecular fluorescence complementation (BiFC) analysis. Max was recruited to different subnuclear locations by interactions with Myc versus Mad family members. Complexes formed by Max with Mxi1, Mad3, or Mad4 were enriched in nuclear foci, whereas complexes formed with Myc were more uniformly distributed in the nucleoplasm. Mad4 was localized to the cytoplasm when it was expressed separately, and Mad4 was recruited to the nucleus through dimerization with Max. The cytoplasmic localization of Mad4 was determined by a CRM1-dependent nuclear export signal located near the amino terminus. We compared the relative efficiencies of complex formation among Myc, Max, and Mad family proteins in living cells using multicolor BiFC analysis. Max formed heterodimers with the basic helix-loop-helix leucine zipper (bHLHZIP) domain of Myc (bMyc) more efficiently than it formed homodimers. Replacement of two amino acid residues in the leucine zipper of Max reversed the relative efficiencies of homo- and heterodimerization in cells. Surprisingly, Mad3 formed complexes with Max less efficiently than bMyc, whereas Mad4 formed complexes with Max more efficiently than bMyc. The distinct subcellular locations and the differences between the efficiencies of dimerization with Max indicate that Mad3 and Mad4 are likely to modulate transcription activation by Myc at least in part through distinct mechanisms.
机译：Myc和Mad家族蛋白在控制细胞生长和增殖中起相反的作用。我们已经可视化使用双分子荧光互补（BiFC）分析由Myc / Max / Mad家族蛋白形成的复合物的亚细胞位置。通过与Myc和Mad家庭成员的互动，Max被招募到不同的亚核位置。 Max与Mxi1，Mad3或Mad4形成的复合物富含核病灶，而与Myc形成的复合物在核质中分布更均匀。分别表达时，Mad4定位在细胞质中，并且通过与Max的二聚化将Mad4募集到细胞核中。 Mad4的胞质定位是由位于氨基末端附近的CRM1依赖性核输出信号决定的。我们使用多色BiFC分析比较了活细胞中Myc，Max和Mad家族蛋白之间复合物形成的相对效率。 Max形成异源二聚体比Myc（bMyc）具有基本的螺旋-环-螺旋亮氨酸拉链（bHLHZIP）结构域的异源二聚体形成异源二聚体的效率更高。 Max亮氨酸拉链中两个氨基酸残基的替换逆转了细胞中同源二聚体和异源二聚体的相对效率。令人惊讶的是，Mad3与Max形成复合物的效率低于bMyc，而Mad4与Max形成复合物的效率低于bMyc。不同的亚细胞位置以及Max的二聚化效率之间的差异表明，Mad3和Mad4可能至少部分通过不同的机制调节Myc的转录激活。

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