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首页> 外文期刊>Molecular biology of the cell >Multiple interactions drive adaptor-mediated recruitment of the ubiquitin ligase Rsp5 to membrane proteins in vivo and in vitro
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Multiple interactions drive adaptor-mediated recruitment of the ubiquitin ligase Rsp5 to membrane proteins in vivo and in vitro

机译：多种相互作用在体内和体外驱动泛素连接酶Rsp5介导的衔接子介导募集到膜蛋白

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摘要

Recognition of membrane proteins by the Nedd4/Rsp5 ubiquitin ligase family is a critical step in their targeting to the multivesicular body pathway. Some substrates contain "PY" motifs (PPxY), which bind to WW domains in the ligase. Others lack PY motifs and instead rely on adaptors that recruit the ligase to them. To investigate the mechanism of adaptor-mediated ubiquitination, we have characterized the interactions between the adaptor Bsd2, the ubiquitin ligase Rsp5, and the membrane proteins Cps1, Tre1, and Smf1 from Saccharomyces cerevisiae. We have reconstituted adaptor-mediated modification of Cps1 and Tre1 in vitro, and we show that two PY motifs in Bsd2 and two WW domains (WW2 and WW3) in Rsp5 are crucial for this. The binding of a weak noncanonical DMAPSY motif in Bsd2 to WW3 is an absolute requirement for Bsd2 adaptor function. We show that sorting of the manganese transporter Smf1, which requires both Bsd2 and Tre1, depends upon two PY motifs in Bsd2 and one motif in Tre1 but only two WW domains in Rsp5. We suggest that sequential assembly of first a Bsd2/Rsp5 complex, then a Tre1/Bsd2/Rsp5 complex followed by a rearrangement of PY-WW interactions is required for the ubiquitination of Smf1.
机译：Nedd4 / Rsp5泛素连接酶家族对膜蛋白的识别是靶向多囊体途径的关键步骤。一些底物包含与连接酶中的WW结构域结合的“ PY”基序（PPxY）。其他人缺乏PY主题，而是依靠将连接酶募集到它们的衔接子。若要调查适配器介导的泛素化的机制，我们已表征了衔接子Bsd2，泛素连接酶Rsp5与来自酿酒酵母的膜蛋白Cps1，Tre1和Smf1之间的相互作用。我们已经重建了体外介导的Cps1和Tre1的衔接子修饰，并且我们显示Bsd2中的两个PY基序和Rsp5中的两个WW域（WW2和WW3）对此至关重要。 Bsd2中的弱非规范DMAPSY基序与WW3的绑定是Bsd2适配器功能的绝对要求。我们显示，需要Bsd2和Tre1的锰转运蛋白Smf1的排序取决于Bsd2中的两个PY主题和Tre1中的一个主题，但取决于Rsp5中的两个WW域。我们建议先组装一个Bsd2 / Rsp5复合体，然后一个Tre1 / Bsd2 / Rsp5复合体，然后重新排列PY-WW相互作用的顺序组装是Smf1泛素化所必需的。

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