Structural basis for the assembly of the Ragulator-Rag GTPase complex
mTORC1 activity is controlled through Rag GTPases, which are anchored to the lysosome through the Ragulator. Here, the authors give molecular insights into Ragulator-Rag GTPase assembly and present the crystal structures of the Ragulator alone and in complex with the RagA-C roadblock domains.
Guardado en:
Autores principales: | Ryo Yonehara, Shigeyuki Nada, Tomokazu Nakai, Masahiro Nakai, Ayaka Kitamura, Akira Ogawa, Hirokazu Nakatsumi, Keiichi I. Nakayama, Songling Li, Daron M. Standley, Eiki Yamashita, Atsushi Nakagawa, Masato Okada |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2017
|
Materias: | |
Acceso en línea: | https://doaj.org/article/482ae068892c43919082fb767f0bf703 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Structural basis for Ragulator functioning as a scaffold in membrane-anchoring of Rag GTPases and mTORC1
por: Tianlong Zhang, et al.
Publicado: (2017) -
Amino acids stimulate the endosome-to-Golgi trafficking through Ragulator and small GTPase Arl5
por: Meng Shi, et al.
Publicado: (2018) -
The lysosomal Ragulator complex plays an essential role in leukocyte trafficking by activating myosin II
por: Takeshi Nakatani, et al.
Publicado: (2021) -
Limited survival and impaired hepatic fasting metabolism in mice with constitutive Rag GTPase signaling
por: Celia de la Calle Arregui, et al.
Publicado: (2021) -
HIV-1 enhances mTORC1 activity and repositions lysosomes to the periphery by co-opting Rag GTPases
por: Alessandro Cinti, et al.
Publicado: (2017)