ESCRT-III Family Members Stimulate Vps4 ATPase Activity Directly or via Vta1
| Autor: | Brian A. Davies, Zhaohui Xu, David J. Katzmann, Junyu Xiao, Markus Babst, Ishara F. Azmi |
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| Rok vydání: | 2008 |
| Předmět: |
Models
Molecular Saccharomyces cerevisiae Proteins Endosome ATPase Viral budding Vesicular Transport Proteins Nerve Tissue Proteins Saccharomyces cerevisiae macromolecular substances General Biochemistry Genetics and Molecular Biology ESCRT Downregulation and upregulation Biomarkers Tumor Binding site Molecular Biology Adenosine Triphosphatases Binding Sites Endosomal Sorting Complexes Required for Transport biology Cell Biology Cell biology Kinetics Protein Subunits biology.protein Cytokinesis Function (biology) Plasmids Developmental Biology |
| Zdroj: | Developmental Cell. 14:50-61 |
| ISSN: | 1534-5807 |
| Popis: | The AAA-ATPase Vps4 is critical for function of the MVB sorting pathway, which in turn impacts cellular phenomena ranging from receptor downregulation to viral budding to cytokinesis. Vps4 dissociates ESCRTs from endosomal membranes during MVB sorting, but it is unclear how Vps4 ATPase activity is synchronized with ESCRT release. Vta1 potentiates Vps4 activity and interacts with ESCRT-III family members. We have investigated the impact of Vta1 and ESCRT-III family members on Vps4 ATPase activity. Two distinct mechanisms of Vps4 stimulation are described: Vps2 can directly stimulate Vps4 via its MIT domain, whereas Vps60 stimulates via Vta1. Moreover, Did2 can stimulate Vps4 by both mechanisms in distinct contexts. Recent structural determination of the ESCRT-III-binding region of Vta1 unexpectedly revealed a MIT-like region. These data support a model wherein a network of MIT and MIT-like domain interactions with ESCRT-III subunits contributes to the regulation of Vps4 activity during MVB sorting. |
| Databáze: | OpenAIRE |
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