Cargando…
Structural basis for Ragulator functioning as a scaffold in membrane-anchoring of Rag GTPases and mTORC1
Amino acid-dependent activation of the mechanistic target of rapamycin complex 1 (mTORC1) is mediated by Rag GTPases, which are recruited to the lysosome by the Ragulator complex consisting of p18, MP1, p14, HBXIP and C7orf59; however, the molecular mechanism is elusive. Here, we report the crystal...
Autores principales: | Zhang, Tianlong, Wang, Rong, Wang, Zhijing, Wang, Xiangxiang, Wang, Fang, Ding, Jianping |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2017
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5680233/ https://www.ncbi.nlm.nih.gov/pubmed/29123114 http://dx.doi.org/10.1038/s41467-017-01567-4 |
Ejemplares similares
-
Structural basis for the assembly of the Ragulator-Rag GTPase complex
por: Yonehara, Ryo, et al.
Publicado: (2017) -
A nutrient-induced affinity switch controls mTORC1 activation by its Rag GTPase-Ragulator lysosomal scaffold
por: Lawrence, Rosalie E., et al.
Publicado: (2018) -
Structure of the lysosomal mTORC1–TFEB–Rag–Ragulator megacomplex
por: Cui, Zhicheng, et al.
Publicado: (2023) -
Structural insight into the Ragulator complex which anchors mTORC1 to the lysosomal
membrane
por: Mu, Zongkai, et al.
Publicado: (2017) -
Regulation of mTORC1 by the Rag GTPases
por: Lama-Sherpa, Tshering D., et al.
Publicado: (2023)