Quantitative interaction mapping reveals an extended UBX domain in ASPL that disrupts functional p97 hexamers
The AAA+ ATPase p97 is an essential hexameric protein with multiple protein interaction partners and cellular functions. Here, the authors use interaction mapping to examine partner proteins of this large complex, and assess the effects of these proteins on the disassembly of the p97 complex.
Guardado en:
Autores principales: | Anup Arumughan, Yvette Roske, Carolin Barth, Laura Lleras Forero, Kenny Bravo-Rodriguez, Alexandra Redel, Simona Kostova, Erik McShane, Robert Opitz, Katja Faelber, Kirstin Rau, Thorsten Mielke, Oliver Daumke, Matthias Selbach, Elsa Sanchez-Garcia, Oliver Rocks, Daniela Panáková, Udo Heinemann, Erich E. Wanker |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2016
|
Materias: | |
Acceso en línea: | https://doaj.org/article/c05c3467f02d4df0b4320632445b06fa |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Ubx-Collier signaling cascade maintains blood progenitors in the posterior lobes of the Drosophila larval lymph gland.
por: Aditya Kanwal, et al.
Publicado: (2021) -
Multi-level and lineage-specific interactomes of the Hox transcription factor Ubx contribute to its functional specificity
por: Julie Carnesecchi, et al.
Publicado: (2020) -
ATP synthase hexamer assemblies shape cristae of Toxoplasma mitochondria
por: Alexander Mühleip, et al.
Publicado: (2021) -
Aβ42 pentamers/hexamers are the smallest detectable oligomers in solution
por: Martin Wolff, et al.
Publicado: (2017) -
Bimodal antagonism of PKA signalling by ARHGAP36
por: Rebecca L. Eccles, et al.
Publicado: (2016)