p97 and p47 function in membrane tethering in cooperation with FTCD during mitotic Golgi reassembly

Autor: Yukina Goto, Kyohei Shimoda, Hisao Kondo, Yayoi Kaneko, Xiaodong Zhang, Silvia Panico, Rafael Ayala
Rok vydání: 2021
Předmět:
inorganic chemicals
Ammonia-Lyases
congenital
hereditary
and neonatal diseases and abnormalities
Glutamate Formimidoyltransferase
Golgi Apparatus
Mitosis
Golgi reassembly
Biology
Membrane Fusion
General Biochemistry
Genetics and Molecular Biology
03 medical and health sciences
symbols.namesake
0302 clinical medicine
Golgi membrane fusion
Valosin Containing Protein
hemic and lymphatic diseases
Humans
Molecular Biology
030304 developmental biology
0303 health sciences
Binding Sites
General Immunology and Microbiology
Polyglutamate
General Neuroscience
Lipid bilayer fusion
hemic and immune systems
Biological membrane
Articles
Hep G2 Cells
Golgi apparatus
Multifunctional Enzymes
Mitochondria
Cell biology
Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins
Multiprotein Complexes
symbols
030217 neurology & neurosurgery
Biogenesis
HeLa Cells
Protein Binding
circulatory and respiratory physiology
Zdroj: EMBO J
ISSN: 1460-2075
0261-4189
DOI: 10.15252/embj.2020105853
Popis: 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.
Databáze: OpenAIRE
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