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首页> 外文期刊>Cell and Tissue Research >Nuclear translocation of lysyl oxidase is promoted by interaction with transcription repressor p66β.
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Nuclear translocation of lysyl oxidase is promoted by interaction with transcription repressor p66β.

机译：赖氨酰氧化酶的核易位通过与转录阻遏物p66β的相互作用而促进。

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摘要

Lysyl oxidase (LOX) is an amine oxidase involved in protein cross-linking of the extracellular matrix. Less well characterized is the role that LOX plays among nuclear proteins, and molecular mechanisms of its transport to the nucleus are currently unknown. Here, we have employed yeast two-hybrid library screening and found that the LOX catalytic domain interacts with the transcription repressor p66β. This interaction has been confirmed in vitro and has been found to be accomplished through the CR2-containing domain of p66β. Moreover, co-expression of p66β and LOX in living tumor cells leads to the nuclear accumulation of LOX. Thus, p66β might be important for the regulation of LOX in the nucleus.
机译：赖氨酰氧化酶（LOX）是一种胺氧化酶，参与细胞外基质的蛋白质交联。 LOX在核蛋白中的作用还不太清楚，其转运到细胞核的分子机制目前尚不清楚。在这里，我们采用酵母双杂交文库筛选，发现LOX催化域与转录阻遏物p66β相互作用。这种相互作用已在体外得到证实，并且发现是通过p66β的含CR2结构域完成的。此外，活肿瘤细胞中p66β和LOX的共表达导致LOX的核积累。因此，p66β对于调节细胞核中的LOX可能很重要。

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