Structural basis for the ARF GAP activity and specificity of the C9orf72 complex.
ADP-Ribosylation Factor 1
/ metabolism
Amyotrophic Lateral Sclerosis
/ genetics
Autophagy-Related Proteins
/ genetics
C9orf72 Protein
/ genetics
Carrier Proteins
/ genetics
Cryoelectron Microscopy
Frontotemporal Dementia
/ genetics
Humans
Mechanistic Target of Rapamycin Complex 1
/ metabolism
Multiprotein Complexes
/ genetics
Protein Structure, Tertiary
/ genetics
rab GTP-Binding Proteins
/ metabolism
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
18 06 2021
18 06 2021
Historique:
received:
17
05
2021
accepted:
27
05
2021
entrez:
19
6
2021
pubmed:
20
6
2021
medline:
7
7
2021
Statut:
epublish
Résumé
Mutation of C9ORF72 is the most common genetic cause of amyotrophic lateral sclerosis (ALS) and frontal temporal degeneration (FTD), which is attributed to both a gain and loss of function. C9orf72 forms a complex with SMCR8 and WDR41, which was reported to have GTPase activating protein activity toward ARF proteins, RAB8A, and RAB11A. We determined the cryo-EM structure of ARF1-GDP-BeF
Identifiants
pubmed: 34145292
doi: 10.1038/s41467-021-24081-0
pii: 10.1038/s41467-021-24081-0
pmc: PMC8213707
doi:
Substances chimiques
Autophagy-Related Proteins
0
C9orf72 Protein
0
Carrier Proteins
0
Multiprotein Complexes
0
SMCR8 protein, human
0
WDR41 protein, human
0
Mechanistic Target of Rapamycin Complex 1
EC 2.7.11.1
rab11 protein
EC 3.6.1.-
RAB8A protein, human
EC 3.6.1.-.
ADP-Ribosylation Factor 1
EC 3.6.5.2
ARF1 protein, human
EC 3.6.5.2
rab GTP-Binding Proteins
EC 3.6.5.2
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, Non-P.H.S.
Langues
eng
Sous-ensembles de citation
IM
Pagination
3786Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM111730
Pays : United States
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