Structure and mechanism of the ESCRT pathway AAA+ ATPase Vps4.
AAA proteins
cryo-electron microscopy
endosomal sorting
protein disassembly
protein structure
Journal
Biochemical Society transactions
ISSN: 1470-8752
Titre abrégé: Biochem Soc Trans
Pays: England
ID NLM: 7506897
Informations de publication
Date de publication:
28 02 2019
28 02 2019
Historique:
received:
26
08
2018
revised:
24
10
2018
accepted:
29
10
2018
pubmed:
17
1
2019
medline:
30
4
2019
entrez:
17
1
2019
Statut:
ppublish
Résumé
The progression of ESCRT (Endosomal Sorting Complexes Required for Transport) pathways, which mediate numerous cellular membrane fission events, is driven by the enzyme Vps4. Understanding of Vps4 mechanism is, therefore, of fundamental importance in its own right and, moreover, it is highly relevant to the understanding of many related AAA+ ATPases that function in multiple facets of cell biology. Vps4 unfolds its ESCRT-III protein substrates by translocating them through its central hexameric pore, thereby driving membrane fission and recycling of ESCRT-III subunits. This mini-review focuses on recent advances in Vps4 structure and mechanism, including ideas about how Vps4 translocates and unfolds ESCRT-III subunits. Related AAA+ ATPases that share structural features with Vps4 and likely utilize an equivalent mechanism are also discussed.
Identifiants
pubmed: 30647138
pii: BST20180260
doi: 10.1042/BST20180260
pmc: PMC6393862
doi:
Substances chimiques
Endosomal Sorting Complexes Required for Transport
0
Protein Subunits
0
Vacuolar Proton-Translocating ATPases
EC 3.6.1.-
ATPases Associated with Diverse Cellular Activities
EC 3.6.4.-
VPS4A protein, human
EC 3.6.4.6
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
37-45Informations de copyright
© 2019 The Author(s).
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