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N- and C-terminal Upf1 phosphorylations create binding platforms for SMG-6 and SMG-5:SMG-7 during NMD

机译：NMD期间，N和C端Upf1磷酸化为SMG-6和SMG-5：SMG-7创建结合平台

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摘要

Nonsense-mediated mRNA decay (NMD) is a surveillance mechanism that detects and degrades mRNAs containing premature termination codons (PTCs). SMG-1-mediated Upf1 phosphorylation takes place in the decay inducing complex (DECID), which contains a ribosome, release factors, Upf1, SMG-1, an exon junction complex (EJC) and a PTC-mRNA. However, the significance and the consequence of Upf1 phosphorylation remain to be clarified. Here, we demonstrate that SMG-6 binds to a newly identified phosphorylation site in Upf1 at N-terminal threonine 28, whereas the SMG-5:SMG-7 complex binds to phosphorylated serine 1096 of Upf1. In addition, the binding of the SMG-5:SMG-7 complex to Upf1 resulted in the dissociation of the ribosome and release factors from the DECID complex. Importantly, the simultaneous binding of both the SMG-5:SMG-7 complex and SMG-6 to phospho-Upf1 are required for both NMD and Upf1 dissociation from mRNA. Thus, the SMG-1-mediated phosphorylation of Upf1 creates a binding platforms for the SMG-5:SMG-7 complex and for SMG-6, and triggers sequential remodeling of the mRNA surveillance complex for NMD induction and recycling of the ribosome, release factors and NMD factors.

机译：无意义介导的mRNA衰变（NMD）是一种监视机制，可检测和降解包含过早终止密码子（PTC）的mRNA。 SMG-1介导的Upf1磷酸化发生在衰变诱导复合物（DECID）中，该复合物包含核糖体，释放因子，Upf1，SMG-1，外显子连接复合物（EJC）和PTC-mRNA。但是，Upf1磷酸化的意义和结果仍有待澄清。在这里，我们证明SMG-6在Upf1的N端苏氨酸28上与新鉴定的磷酸化位点结合，而SMG-5：SMG-7复合物则与Upf1的磷酸化丝氨酸1096结合。此外，SMG-5：SMG-7复合物与Upf1的结合导致核糖体和DECID复合物的释放因子解离。重要的是，NMD和Upf1从mRNA分离都需要SMG-5：SMG-7复合物和SMG-6与磷酸Upf1同时结合。因此，Upf1的SMG-1介导的磷酸化为SMG-5：SMG-7复合物和SMG-6创建了结合平台，并触发了mRNA监测复合物的顺序重塑，用于NMD诱导和核糖体的回收，释放。因素和NMD因素。

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Okada-Katsuhata, Yukiko; Yamashita, Akio; Kutsuzawa, Kei; Izumi, Natsuko; Hirahara, Fumiki; Ohno, Shigeo;
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年度 2011
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1. N- and C-terminal Upf1 phosphorylations create binding platforms for SMG-6 and SMG-5:SMG-7 during NMD [J] . Okada-Katsuhata Yukiko, Yamashita Akio, Kutsuzawa Kei, Nucleic Acids Research . 2012,第3期

机译：NMD期间，N和C端Upf1磷酸化为SMG-6和SMG-5：SMG-7创建结合平台
2. N- and C-terminal Upf1 phosphorylations create binding platforms for SMG-6 and SMG-5:SMG-7 during NMD [J] . Akio Yamashita, Fumiki Hirahara, Kei Kutsuzawa, Nucleic acids research . 2012,第3期

机译：NMD期间，N和C端Upf1磷酸化为SMG-6和SMG-5：SMG-7创建结合平台
3. A novel phosphorylation-independent interaction between SMG6 and UPF1 is essential for human NMD [J] . Nicholson Pamela, Josi Christoph, Kurosawa Hitomi, Nucleic Acids Research . 2014,第14期

机译：SMG6和UPF1之间的新型磷酸化无关的相互作用对于人NMD至关重要
4. Phosphorylation of the C-terminal PSD-95/discs large/zona occludens-1 (PDZ) binding site of stargazin regulates its trafficking in bidirectional synaptic plasticity. [D] . Stein, Emma Leigh Ann. 2009

机译：Stargazin的C端PSD-95 / discs大/ zona occludens-1（PDZ）结合位点的磷酸化调节了其在双向突触可塑性中的运输。
5. N- and C-terminal Upf1 phosphorylations create binding platforms for SMG-6 and SMG-5:SMG-7 during NMD [O] . Yukiko Okada-Katsuhata, Akio Yamashita, Kei Kutsuzawa, 2012

机译：NMD期间N和C端Upf1磷酸化为SMG-6和SMG-5：SMG-7创建结合平台
6. Phosphorylation of the N- and C-terminal UPF1 domains plays a critical role in plant nonsense-mediated mRNA decay [O] . Kerényi, Farkas, Wawer, Izabela, Sikorski, Pawel J., 2017

机译：N-和C-末端UpF1结构域的磷酸化在植物无义介导的mRNa衰变中起关键作用

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