The N-terminal leucine-zipper motif in PTRF/cavin-1 is essential and sufficient for its caveolae-association
The N-terminal leucine-zipper motif in PTRF/cavin-1 is essential and sufficient for its caveolae-association
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PTRF/cavin-1 中的 N 端亮氨酸拉链基序对于其小窝关联至关重要且足够
DOI：
10.1016/j.bbrc.2014.12.035
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发表时间：
2015-01-16
影响因子：
3.1
通讯作者：
Liao, Ion
中科院分区：
文献类型：
--
作者：
Wei, Zhuang;Zou, Xinle;Liao, Ion
PTRF/cavin-1是两种生命的蛋白质。据报道，它在核糖体RNA合成和小窝形成中的功能发生在两个不同的细胞位置：细胞核与质膜。在这里，我们确定了PTRF/cavin-1的N-末端亮氨酸拉链基序是必不可少的蛋白质与质膜小窝。它可以抵消分子中的核定位序列（AA 235-251）的作用。从PTRF/cavin-1中删除这个亮氨酸拉链基序导致突变体仅定位于细胞核中。该亮氨酸拉链基序与核蛋白组蛋白2A融合，可诱导融合蛋白从核中输出。在PTRF/cavin-1（-/-）小鼠胚胎成纤维细胞（MEFs）中，细胞迁移被极大地抑制。被抑制的细胞运动只能由外源性cavin-1拯救，而不是亮氨酸拉链基序缺失的cavin-1突变体。质膜动力学是细胞运动控制的重要因素。我们的研究结果表明，细胞迁移中的膜动力学受到小窝相关的PTRF/cavin-1的影响。(C)2014爱思唯尔公司All rights reserved.
PTRF/cavin-1 is a protein of two lives. Its reported functions in ribosomal RNA synthesis and in caveolae formation happen in two different cellular locations: nucleus vs. plasma membrane. Here, we identified that the N-terminal leucine-zipper motif in PTRF/cavin-1 was essential for the protein to be associated with caveolae in plasma membrane. It could counteract the effect of nuclear localization sequence in the molecule (AA 235-251). Deletion of this leucine-zipper motif from PTRF/cavin-1 caused the mutant to be exclusively localized in nuclei. The fusion of this leucine-zipper motif with histone 2A, which is a nuclear protein, could induce the fusion protein to be exported from nucleus. Cell migration was greatly inhibited in PTRF/cavin-1(-/-) mouse embryonic fibroblasts (MEFs). The inhibited cell motility could only be rescued by exogenous cavin-1 but not the leucine-zipper motif deleted cavin-1 mutant. Plasma membrane dynamics is an important factor in cell motility control. Our results suggested that the membrane dynamics in cell migration is affected by caveolae associated PTRF/cavin-1. (C) 2014 Elsevier Inc. All rights reserved.