Cargando…
Novel regulatory roles of Mff and Drp1 in E3 ubiquitin ligase MARCH5–dependent degradation of MiD49 and Mcl1 and control of mitochondrial dynamics
MARCH5, an OMM-associated E3 ubiquitin ligase, controls mitochondrial function. Despite its importance, the mechanism and factors controlling MARCH5 activity are largely unknown. Here we report that the MARCH5 C-terminal domain plays a critical role in degradation of MARCH5 substrates, likely by fac...
Autores principales: | Cherok, Edward, Xu, Shan, Li, Sunan, Das, Shweta, Meltzer, W. Alex, Zalzman, Michal, Wang, Chunxin, Karbowski, Mariusz |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The American Society for Cell Biology
2017
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5341724/ https://www.ncbi.nlm.nih.gov/pubmed/27932492 http://dx.doi.org/10.1091/mbc.E16-04-0208 |
Ejemplares similares
-
Mitochondrial E3 ubiquitin ligase MARCH5 controls mitochondrial fission and cell sensitivity to stress-induced apoptosis through regulation of MiD49 protein
por: Xu, Shan, et al.
Publicado: (2016) -
The mitochondrial E3 ubiquitin ligase MARCH5 is required for Drp1 dependent mitochondrial division
por: Karbowski, Mariusz, et al.
Publicado: (2007) -
Fis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial fission
por: Losón, Oliver C., et al.
Publicado: (2013) -
Mff is an essential factor for mitochondrial recruitment of Drp1 during mitochondrial fission in mammalian cells
por: Otera, Hidenori, et al.
Publicado: (2010) -
The mitochondrial fission receptor Mff selectively recruits oligomerized Drp1
por: Liu, Raymond, et al.
Publicado: (2015)