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首页> 外文期刊>Cell cycle >TRIP6 and LPP, but not Zyxin, are present at a subset of telomeres in human cells.
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TRIP6 and LPP, but not Zyxin, are present at a subset of telomeres in human cells.

机译：TRIP6和LPP，而不是Zyxin，存在于人类细胞的端粒子集中。

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摘要

The protection of chromosome ends requires the inhibition of DNA damage responses at telomeres. This inhibition is exerted in great part by the shelterin complex, known to prevent inappropriate ATM and ATR activation. The molecular mechanisms by which shelterin protects telomeres are incompletely understood. Recently, we have implicated for the first time a class of molecules, LIM domain proteins, in telomere protection. This protection occurred through interaction with shelterin, possibly through POT1, and required the pair of LIM proteins TRIP6 and LPP, themselves part of the Zyxin family. The domain similarity between TRIP6, LPP and Zyxin led us to ask whether the latter also interacted with telomeres. Here, we show that there is specificity in the association of LIM proteins with telomeres: Zyxin, despite a high degree of similarity with TRIP6 and LPP, was not detected at telomeres, nor found in a complex with shelterin. TRIP6 and LPP, however, were detected by immunofluorescence at a small subset of telomeres, perhaps those that are critically short. We speculate that specific LIM proteins are part of complex events occurring in the context of the telomere dysfunction response, and possibly at play during the induction of senescence.
机译：保护染色体末端需要抑制端粒处的DNA损伤反应。这种抑制作用在很大程度上由防护素复合物施加，已知该复合物可防止不适当的ATM和ATR激活。庇护素保护端粒的分子机制尚不完全清楚。最近，我们首次涉及端粒保护中的一类分子，LIM域蛋白。这种保护作用是通过与庇护素相互作用（可能是通过POT1）而发生的，并且需要一对ZIM家族的LIM蛋白TRIP6和LPP。 TRIP6，LPP和合酶之间的结构域相似性导致我们问后者是否也与端粒相互作用。在这里，我们显示LIM蛋白与端粒的缔合具有特异性：Zyxin，尽管与TRIP6和LPP具有高度相似性，但在端粒中未检测到，也未在庇护蛋白复合物中发现。然而，通过免疫荧光检测在一小部分端粒中可能检测到TRIP6和LPP，这些端粒可能非常短。我们推测，特定的LIM蛋白是端粒功能障碍反应中发生的复杂事件的一部分，并且可能在衰老诱导过程中发挥作用。

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