Recycling of ESCRTs by the AAA-ATPase Vps4 is regulated by a conserved VSL region in Vta1.

Recycling of ESCRTs by the AAA-ATPase Vps4 is regulated by a conserved VSL region in Vta1.
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DOI:
10.1083/jcb.200508166
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发表时间:
2006-02-27
期刊:
The Journal of cell biology
影响因子:
--
通讯作者:
Katzmann DJ
Katzmann DJ
中科院分区:
其他
文献类型:
--
作者:
Azmi I;Davies B;Dimaano C;Payne J;Eckert D;Babst M;Katzmann DJ

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在真核生物中,多泡体(MVB)分选途径在调节细胞表面蛋白质组成中起重要作用,从而影响许多细胞功能。Vps 4是一种与多种细胞活性相关的ATP酶,在MVB分选反应后期需要Vps 4来解离转运所需的内体分选复合物(ESCRT),这是该途径正常功能的必要条件。然而,Vps 4功能的调节尚不清楚。我们的特点Vta 1作为一个积极的调节Vps 4在体内和体外。Vta 1促进Vps 4的正确组装,并通过整个进化过程中Vta 1同源物(包括人SBP 1和拟南芥LIP 5)中存在的保守Vta 1/SBP 1/LIP 5区域刺激其ATP酶活性。这些结果表明,通过ESCRT蛋白的拆卸,从而MVB分选,调节Vta 1/SBP 1/LIP 5蛋白的进化保守的机制。
In eukaryotes, the multivesicular body (MVB) sorting pathway plays an essential role in regulating cell surface protein composition, thereby impacting numerous cellular functions. Vps4, an ATPase associated with a variety of cellular activities, is required late in the MVB sorting reaction to dissociate the endosomal sorting complex required for transport (ESCRT), a requisite for proper function of this pathway. However, regulation of Vps4 function is not understood. We characterize Vta1 as a positive regulator of Vps4 both in vivo and in vitro. Vta1 promotes proper assembly of Vps4 and stimulates its ATPase activity through the conserved Vta1/SBP1/LIP5 region present in Vta1 homologues across evolution, including human SBP1 and Arabidopsis thaliana LIP5. These results suggest an evolutionarily conserved mechanism through which the disassembly of the ESCRT proteins, and thereby MVB sorting, is regulated by the Vta1/SBP1/LIP5 proteins.
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