Global phosphoproteomic analysis reveals ARMC10 as an AMPK substrate that regulates mitochondrial dynamics
AMPK is regulates cellular energy and has been extensively studied, although our knowledge of downstream substrates is incomplete. Here, Chen et al. perform global quantitative analysis for AMPK-dependent sites and validate one hit, ARMC10, as a direct AMPK effector of mitochondrial dynamics.
Guardado en:
Autores principales: | Zhen Chen, Caoqi Lei, Chao Wang, Nan Li, Mrinal Srivastava, Mengfan Tang, Huimin Zhang, Jong Min Choi, Sung Yun Jung, Jun Qin, Junjie Chen |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2019
|
Materias: | |
Acceso en línea: | https://doaj.org/article/c4d35187bada4634b09ee0cf3c4b49b5 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
ARMC Subfamily: Structures, Functions, Evolutions, Interactions, and Diseases
por: Yutao Huang, et al.
Publicado: (2021) -
Armc5 deletion causes developmental defects and compromises T-cell immune responses
por: Yan Hu, et al.
Publicado: (2017) -
Potent PDE4 inhibitor activates AMPK and Sirt1 to induce mitochondrial biogenesis.
por: Sung-Jun Park, et al.
Publicado: (2021) -
Epe1 contributes to activation of AMPK by promoting phosphorylation of AMPK alpha subunit, Ssp2
por: Yongyi Chen, et al.
Publicado: (2017) -
A Decade of Pollen Phosphoproteomics
por: Božena Klodová, et al.
Publicado: (2021)