Cargando…
Quantitative interaction mapping reveals an extended UBX domain in ASPL that disrupts functional p97 hexamers
Interaction mapping is a powerful strategy to elucidate the biological function of protein assemblies and their regulators. Here, we report the generation of a quantitative interaction network, directly linking 14 human proteins to the AAA+ ATPase p97, an essential hexameric protein with multiple ce...
Autores principales: | Arumughan, Anup, Roske, Yvette, Barth, Carolin, Forero, Laura Lleras, Bravo-Rodriguez, Kenny, Redel, Alexandra, Kostova, Simona, McShane, Erik, Opitz, Robert, Faelber, Katja, Rau, Kirstin, Mielke, Thorsten, Daumke, Oliver, Selbach, Matthias, Sanchez-Garcia, Elsa, Rocks, Oliver, Panáková, Daniela, Heinemann, Udo, Wanker, Erich E. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2016
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5080433/ https://www.ncbi.nlm.nih.gov/pubmed/27762274 http://dx.doi.org/10.1038/ncomms13047 |
Ejemplares similares
-
Structural remodeling of AAA+ ATPase p97 by adaptor protein ASPL facilitates posttranslational methylation by METTL21D
por: Petrović, Saša, et al.
Publicado: (2023) -
Human ASPL/TUG interacts with p97 and complements the proteasome mislocalization of a yeast ubx4 mutant, but not the ER-associated degradation defect
por: Madsen, Louise, et al.
Publicado: (2014) -
Regulation of Ubx Expression by Epigenetic Enhancer Silencing in Response to Ubx Levels and Genetic Variation
por: Crickmore, Michael A., et al.
Publicado: (2009) -
Multiple UBX proteins reduce the ubiquitin threshold of the mammalian p97-UFD1-NPL4 unfoldase
por: Fujisawa, Ryo, et al.
Publicado: (2022) -
The UBX domain in UBXD1 organizes ubiquitin binding at the C-terminus of the VCP/p97 AAA-ATPase
por: Blueggel, Mike, et al.
Publicado: (2023)