Recognition and Chaperoning by Pex19, Followed by Trafficking and Membrane Insertion of the Peroxisome Proliferation Protein, Pex11.
Recognition and Chaperoning by Pex19, Followed by Trafficking and Membrane Insertion of the Peroxisome Proliferation Protein, Pex11.
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DOI：
10.3390/cells11010157
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发表时间：
2022-01-04
期刊：
影响因子：
6
通讯作者：
Subramani S
中科院分区：
文献类型：
--
作者：
Zientara-Rytter KM;Mahalingam SS;Farré JC;Carolino K;Subramani S
Pex11是一种丰富的过氧体膜蛋白(PMP)，是过氧化体分裂所必需的，并被强健地输入到过氧体的膜上。我们全面分析了毕赤酵母Pex11是如何被Pex19识别和伴随、靶向于过氧化物酶体膜并插入其中的。我们证明了Pex11含有一个Pex19结合位点(Pex19-BS)，这是Pex19将Pex11插入到过氧化体膜中所必需的，但对于过氧化体的运输并不是必需的。我们提供了关于Pex19识别Pex11中Pex19-BS的广泛突变分析。Pex11还具有第二个非依赖于Pex19的膜过氧化体靶向信号，该信号在Pex11家族蛋白中被保存，并将人的HsPex11γ锚定在过氧体膜的外层小叶上。因此，与大多数PMP不同的是，Pex11可以使用两种机制向过氧酶体转运，其中只有一种依赖于它与Pex19的直接相互作用，而另一种不依赖于Pex19。然而，Pex19是Pex11膜插入所必需的。我们证明了Pex11可以通过与其N-末端螺旋结构域的同型和/或异型相互作用进行自我作用。我们证明了Pex19通过与Pex11中的Pex19-BS相互作用而发挥伴侣作用，从而保护Pex11免受自发寡聚的影响，否则会导致Pex11的聚集和随后的降解。
Pex11, an abundant peroxisomal membrane protein (PMP), is required for division of peroxisomes and is robustly imported to peroxisomal membranes. We present a comprehensive analysis of how the Pichia pastoris Pex11 is recognized and chaperoned by Pex19, targeted to peroxisome membranes and inserted therein. We demonstrate that Pex11 contains one Pex19-binding site (Pex19-BS) that is required for Pex11 insertion into peroxisomal membranes by Pex19, but is non-essential for peroxisomal trafficking. We provide extensive mutational analyses regarding the recognition of Pex19-BS in Pex11 by Pex19. Pex11 also has a second, Pex19-independent membrane peroxisome-targeting signal (mPTS) that is preserved among Pex11-family proteins and anchors the human HsPex11γ to the outer leaflet of the peroxisomal membrane. Thus, unlike most PMPs, Pex11 can use two mechanisms of transport to peroxisomes, where only one of them depends on its direct interaction with Pex19, but the other does not. However, Pex19 is necessary for membrane insertion of Pex11. We show that Pex11 can self-interact, using both homo- and/or heterotypic interactions involving its N-terminal helical domains. We demonstrate that Pex19 acts as a chaperone by interacting with the Pex19-BS in Pex11, thereby protecting Pex11 from spontaneous oligomerization that would otherwise cause its aggregation and subsequent degradation.
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