p97 and p47 function in membrane tethering in cooperation with FTCD during mitotic Golgi reassembly.
EMBO J
; 40(9): e105853, 2021 05 03.
Article
em En
| MEDLINE
| ID: mdl-33555040
ABSTRACT
p97ATPase-mediated membrane fusion is required for the biogenesis of the Golgi complex. p97 and its cofactor p47 function in soluble N-ethylmaleimide-sensitive factor (NSF) attachment protein receptor (SNARE) priming, but the tethering complex for p97/p47-mediated membrane fusion remains unknown. In this study, we identified formiminotransferase cyclodeaminase (FTCD) as a novel p47-binding protein. FTCD mainly localizes to the Golgi complex and binds to either p47 or p97 via its association with their polyglutamate motifs. FTCD functions in p97/p47-mediated Golgi reassembly at mitosis in vivo and in vitro via its binding to p47 and to p97. We also showed that FTCD, p47, and p97 form a big FTCD-p97/p47-FTCD tethering complex. In vivo tethering assay revealed that FTCD that was designed to localize to mitochondria caused mitochondria aggregation at mitosis by forming a complex with endogenous p97 and p47, which support a role for FTCD in tethering biological membranes in cooperation with the p97/p47 complex. Therefore, FTCD is thought to act as a tethering factor by forming the FTCD-p97/p47-FTCD complex in p97/p47-mediated Golgi membrane fusion.
Palavras-chave
Texto completo:
1
Bases de dados:
MEDLINE
Assunto principal:
Glutamato Formimidoiltransferase
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Proteínas de Ligação a Fator Solúvel Sensível a N-Etilmaleimida
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Enzimas Multifuncionais
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Proteína com Valosina
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Complexo de Golgi
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Amônia-Liases
Tipo de estudo:
Prognostic_studies
Limite:
Humans
Idioma:
En
Revista:
EMBO J
Ano de publicação:
2021
Tipo de documento:
Article
País de afiliação:
Japão