Cryo-EM Structure of Dodecameric Vps4p and Its 2:1 Complex with Vta1p

The type I AAA (ATPase associated with a variety of cellular activities) ATPase Vps4 and its co-factor Vta1p/LIP5 function in membrane remodeling events that accompany cytokinesis, multivesicular body biogenesis, and retrovirus budding, apparently by driving disassembly and recycling of membrane-ass...

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Bibliographic Details
Published in:Journal of molecular biology 2008-03, Vol.377 (2), p.364-377
Main Authors: Yu, Zhiheng, Gonciarz, Malgorzata D., Sundquist, Wesley I., Hill, Christopher P., Jensen, Grant J.
Format: Article
Language:English
Subjects:
AAA ATPase
Adenosine Triphosphatases - chemistry
Adenosine Triphosphatases - genetics
Adenosine Triphosphatases - metabolism
Adenosine Triphosphatases - ultrastructure
Chromatography, Gel
Cryo-EM
Cryoelectron Microscopy
Endosomal Sorting Complexes Required for Transport
HIV budding
Models, Molecular
Protein Binding
Protein Structure, Quaternary
Saccharomyces cerevisiae - chemistry
Saccharomyces cerevisiae - enzymology
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae - ultrastructure
Saccharomyces cerevisiae Proteins - chemistry
Saccharomyces cerevisiae Proteins - genetics
Saccharomyces cerevisiae Proteins - metabolism
Saccharomyces cerevisiae Proteins - ultrastructure
Vesicular Transport Proteins - chemistry
Vesicular Transport Proteins - genetics
Vesicular Transport Proteins - metabolism
Vesicular Transport Proteins - ultrastructure
Vps4
Vta1
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Summary:The type I AAA (ATPase associated with a variety of cellular activities) ATPase Vps4 and its co-factor Vta1p/LIP5 function in membrane remodeling events that accompany cytokinesis, multivesicular body biogenesis, and retrovirus budding, apparently by driving disassembly and recycling of membrane-associated ESCRT (endosomal sorting complex required for transport)-III complexes. Here, we present electron cryomicroscopy reconstructions of dodecameric yeast Vps4p complexes with and without their microtubule interacting and transport (MIT) N-terminal domains and Vta1p co-factors. The ATPase domains of Vps4p form a bowl-like structure composed of stacked hexameric rings. The two rings adopt dramatically different conformations, with the “upper” ring forming an open assembly that defines the sides of the bowl and the lower ring forming a closed assembly that forms the bottom of the bowl. The N-terminal MIT domains of the upper ring localize on the symmetry axis above the cavity of the bowl, and the binding of six extended Vta1p monomers causes additional density to appear both above and below the bowl. The structures suggest models in which Vps4p MIT and Vta1p domains engage ESCRT-III substrates above the bowl and help transfer them into the bowl to be pumped through the center of the dodecameric assembly.
ISSN:0022-2836
1089-8638
DOI:10.1016/j.jmb.2008.01.009