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

JOURNAL OF MOLECULAR BIOLOGY

卷:377

Article

Hartmann, Claudia^1,2  Chami, Mohamed¹  Zachariae, Ulrich³  de Groot, Bert L.³  Engel, Andreas¹  Gruetter, Markus G.² 

[1] Univ Basel, Biozentrum, ME Inst Struct Biol, CH-4056 Basel, Switzerland

[2] Univ Zurich, Inst Biochem, CH-8057 Zurich, Switzerland

[3] Max Planck Inst Biophys Chem, D-37077 Gottingen, Germany

关键词: ESCRT;    membrane traffic;    HIV;    AAA-ATPase;    Vps;   

DOI  :  10.1016/j.jmb.2008.01.010

来源: Elsevier

【 摘 要 】

The vacuolar protein sorting (Vps) pathway, in which Vps4 class I AAA-ATPases 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 atonLic structure of the nucleotide-free yeast HiS(6)Delta NVps4p dimer and its AMPPNP (5'-adenylyl-beta,gamma-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 11 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. (C) 2008 Elsevier Ltd. All rights reserved.

【 授权许可】

Free