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Wilbrey, Anna L.; Haley, Jane E.; Wishart, Thomas M.; Conforti, Laura; Morreale, Giacomo; Beirowski, Bogdan; Babetto, Elisabetta; Adalbert, Robert; Gillingwater, Thomas H.; Smith, Trevor; Wyllie, David J.A.; Ribchester, Richard R.; Coleman, Michael P.
Molecular and cellular neuroscience, 2008, Letnik: 38, Številka: 3Journal Article
Wallerian degeneration slow (Wld S) mice express a chimeric protein that delays axonal degeneration. The N-terminal domain (N70), which is essential for axonal protection in vivo, binds valosin-containing protein (VCP) and targets both Wld S and VCP to discrete nuclear foci. We characterized the formation, composition and localization of these potentially important foci. Missense mutations show that the N-terminal sixteen residues (N16) of Wld S are essential for both VCP binding and targeting Wld S to nuclear foci. Removing N16 abolishes foci, and VCP binding sequences from ataxin-3 or HrdI restore them. In vitro, these puncta co-localize with proteasome subunits. In vivo, Wld S assumes a range of nuclear distribution patterns, including puncta, and its neuronal expression and intranuclear distribution is region-specific and varies between spontaneous and transgenic Wld S models. We conclude that VCP influences Wld S intracellular distribution, and thus potentially its function, by binding within the N70 domain required for axon protection.
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Leto | Faktor vpliva | Izdaja | Kategorija | Razvrstitev | ||||
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JCR | SNIP | JCR | SNIP | JCR | SNIP | JCR | SNIP |
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Vir: Osebne bibliografije
in: SICRIS
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