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Vacuolar protein sorting: two different functional states of the AAA-ATPase Vps4p


Hartmann, C; Chami, M; Zachariae, U; de Groot, B L; Engel, A; Grütter, M G (2008). Vacuolar protein sorting: two different functional states of the AAA-ATPase Vps4p. Journal of Molecular Biology, 377(2):352-363.

Abstract

The vacuolar protein sorting (Vps) pathway, in which Vps4 class I AAAATPases play a central role, regulates growth factor receptors, immune response, and developmental signaling, and participates in tumor suppression, apoptosis, and retrovirus budding. We present the first atomic structure of the nucleotide-free yeast His6ΔNVps4p dimer and its AMPPNP (5′- adenylyl β,γ-imidodiphosphate)-bound tetradecamer, derived from a cryo electron microscopy map. Vps4p dimers form two distinct heptameric rings and accommodate AAA cassettes in a head-to-head—not in a head-to-tail— fashion as in class II AAA-ATPases. Our model suggests a mechanism for
disassembling ESCRT (endosomal sorting complex required for transport) complexes by movements of substrate-binding domains located at the periphery of the tetradecamer during ATP hydrolysis in one ring, followed by translocation through the central pore and ATP hydrolysis in the second
ring.

Abstract

The vacuolar protein sorting (Vps) pathway, in which Vps4 class I AAAATPases play a central role, regulates growth factor receptors, immune response, and developmental signaling, and participates in tumor suppression, apoptosis, and retrovirus budding. We present the first atomic structure of the nucleotide-free yeast His6ΔNVps4p dimer and its AMPPNP (5′- adenylyl β,γ-imidodiphosphate)-bound tetradecamer, derived from a cryo electron microscopy map. Vps4p dimers form two distinct heptameric rings and accommodate AAA cassettes in a head-to-head—not in a head-to-tail— fashion as in class II AAA-ATPases. Our model suggests a mechanism for
disassembling ESCRT (endosomal sorting complex required for transport) complexes by movements of substrate-binding domains located at the periphery of the tetradecamer during ATP hydrolysis in one ring, followed by translocation through the central pore and ATP hydrolysis in the second
ring.

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Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:04 Faculty of Medicine > Department of Biochemistry
07 Faculty of Science > Department of Biochemistry
Dewey Decimal Classification:570 Life sciences; biology
Language:English
Date:21 March 2008
Deposited On:17 Dec 2008 14:26
Last Modified:18 Feb 2018 09:54
Publisher:Elsevier
ISSN:0022-2836
OA Status:Closed
Publisher DOI:https://doi.org/10.1016/j.jmb.2008.01.010
PubMed ID:18272179

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