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首页> 外文期刊>The FEBS journal >The beta domain is required for Vps4p oligomerization into a functionally active ATPase
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The beta domain is required for Vps4p oligomerization into a functionally active ATPase

机译：Vps4p寡聚为功能性活性ATPase所需的beta结构域

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Endocytic and biosynthetic trafficking pathways to the lysosome/vacuole converge at the prevacuolar endosomal compartment. During transport through this compartment, integral membrane proteins that are destined for delivery to the lysosome/vacuole lumen undergo multivesicular body (MVB) sorting into internal vesicles formed by invagination of the endosomal limiting membrane. Vps4 is an AAA family ATPase which plays a key role in MVB sorting and facilitates transport through endosomes. It possesses an N-terminal microtubule interacting and trafficking domain required for recruitment to endosomes and an AAA domain with an ATPase catalytic site. The recently solved 3D structure revealed a P domain, which protrudes from the AAA domain, and a final C-terminal alpha-helix. However, the in vivo roles of these domains are not known. In this study, we have identified motifs in these domains that are highly conserved between yeast and human Vps4. We have mutated these motifs and studied the effect on yeast Vps4p function in vivo and in vitro. We show that the P domain of the budding yeast Vps4p is not required for recruitment to endosomes, but is essential for all Vps4p endocytic functions in vivo. We also show that the P domain is required for Vps4p homotypic interaction and for full ATPase activity. In addition, it is required for interaction with Vta1p, which works in concert with Vps4p in vivo. Our studies suggest that assembly of a Vps4p oligomeric complex with full ATPase activity that interacts with Vta1p is essential for normal endosome function.
机译：溶酶体/真空的内吞和生物合成运输途径在真空前的内体室中汇合。在通过该隔室的运输过程中，注定要递送至溶酶体/真空管腔的完整膜蛋白会经历多囊泡体（MVB）的作用，分选为由内体限制膜的内陷形成的内部囊泡。 Vps4是AAA家族的ATPase，在MVB分选中起关键作用，并有助于通过内体运输。它具有募集至内体所需的N末端微管相互作用和运输结构域，以及具有ATPase催化位点的AAA结构域。最近解决的3D结构显示了一个从AAA域突出的P域和一个最终的C端α螺旋。但是，这些域的体内作用尚不清楚。在这项研究中，我们已经确定了这些域中在酵母和人Vps4之间高度保守的基序。我们已经突变了这些基序，并在体内和体外研究了对酵母Vps4p功能的影响。我们表明，发芽酵母Vps4p的P结构域对于募集到内体不是必需的，但是对于体内的所有Vps4p内吞功能都是必不可少的。我们还显示P域是Vps4p同型相互作用和完整ATPase活性所必需的。此外，与Vta1p相互作用是必需的，后者在体内与Vps4p协同工作。我们的研究表明，具有完整ATPase活性且与Vta1p相互作用的Vps4p寡聚复合物的组装对于正常的内体功能至关重要。

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