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.

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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:	Science Q
Acceso en línea:	https://doaj.org/article/482ae068892c43919082fb767f0bf703
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spelling	oai:doaj.org-article:482ae068892c43919082fb767f0bf7032021-12-02T15:37:06ZStructural basis for the assembly of the Ragulator-Rag GTPase complex10.1038/s41467-017-01762-32041-1723https://doaj.org/article/482ae068892c43919082fb767f0bf7032017-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-017-01762-3https://doaj.org/toc/2041-1723mTORC1 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.Ryo YoneharaShigeyuki NadaTomokazu NakaiMasahiro NakaiAyaka KitamuraAkira OgawaHirokazu NakatsumiKeiichi I. NakayamaSongling LiDaron M. StandleyEiki YamashitaAtsushi NakagawaMasato OkadaNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-11 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q 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 Structural basis for the assembly of the Ragulator-Rag GTPase complex
description	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.
format	article
author	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
author_facet	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
author_sort	Ryo Yonehara
title	Structural basis for the assembly of the Ragulator-Rag GTPase complex
title_short	Structural basis for the assembly of the Ragulator-Rag GTPase complex
title_full	Structural basis for the assembly of the Ragulator-Rag GTPase complex
title_fullStr	Structural basis for the assembly of the Ragulator-Rag GTPase complex
title_full_unstemmed	Structural basis for the assembly of the Ragulator-Rag GTPase complex
title_sort	structural basis for the assembly of the ragulator-rag gtpase complex
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/482ae068892c43919082fb767f0bf703
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Structural basis for the assembly of the Ragulator-Rag GTPase complex

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