Structural basis for Ragulator functioning as a scaffold in membrane-anchoring of Rag GTPases and mTORC1

Activated Rag GTPases recruit mTORC1 to lysosomes. Here the authors present the crystal structure of the Ragulator complex and identify the binding sites for the Roadblock domains of Rag GTPases, which gives insights how Rag GTPases are tethered to the lysosomal membrane.

Bibliographic Details
Main Authors:	Tianlong Zhang, Rong Wang, Zhijing Wang, Xiangxiang Wang, Fang Wang, Jianping Ding
Format:	Article
Language:	English
Published:	Nature Publishing Group 2017-11-01
Series:	Nature Communications
Online Access:	https://doi.org/10.1038/s41467-017-01567-4

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spelling	doaj-b4e9df9de3bc4569a620c6e7d018eab22021-05-11T07:10:18ZengNature Publishing GroupNature Communications2041-17232017-11-018111010.1038/s41467-017-01567-4Structural basis for Ragulator functioning as a scaffold in membrane-anchoring of Rag GTPases and mTORC1Tianlong Zhang0Rong Wang1Zhijing Wang2Xiangxiang Wang3Fang Wang4Jianping Ding5State Key Laboratory of Molecular Biology, National Center for Protein Science Shanghai, Shanghai Science Research Center, CAS Center for Excellence in Molecular Cell Science, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, University of Chinese Academy of Sciences, Chinese Academy of SciencesState Key Laboratory of Molecular Biology, National Center for Protein Science Shanghai, Shanghai Science Research Center, CAS Center for Excellence in Molecular Cell Science, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, University of Chinese Academy of Sciences, Chinese Academy of SciencesState Key Laboratory of Molecular Biology, National Center for Protein Science Shanghai, Shanghai Science Research Center, CAS Center for Excellence in Molecular Cell Science, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, University of Chinese Academy of Sciences, Chinese Academy of SciencesSchool of Life Sciences, Shanghai UniversityState Key Laboratory of Molecular Biology, National Center for Protein Science Shanghai, Shanghai Science Research Center, CAS Center for Excellence in Molecular Cell Science, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, University of Chinese Academy of Sciences, Chinese Academy of SciencesState Key Laboratory of Molecular Biology, National Center for Protein Science Shanghai, Shanghai Science Research Center, CAS Center for Excellence in Molecular Cell Science, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, University of Chinese Academy of Sciences, Chinese Academy of SciencesActivated Rag GTPases recruit mTORC1 to lysosomes. Here the authors present the crystal structure of the Ragulator complex and identify the binding sites for the Roadblock domains of Rag GTPases, which gives insights how Rag GTPases are tethered to the lysosomal membrane.https://doi.org/10.1038/s41467-017-01567-4
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Tianlong Zhang Rong Wang Zhijing Wang Xiangxiang Wang Fang Wang Jianping Ding
spellingShingle	Tianlong Zhang Rong Wang Zhijing Wang Xiangxiang Wang Fang Wang Jianping Ding Structural basis for Ragulator functioning as a scaffold in membrane-anchoring of Rag GTPases and mTORC1 Nature Communications
author_facet	Tianlong Zhang Rong Wang Zhijing Wang Xiangxiang Wang Fang Wang Jianping Ding
author_sort	Tianlong Zhang
title	Structural basis for Ragulator functioning as a scaffold in membrane-anchoring of Rag GTPases and mTORC1
title_short	Structural basis for Ragulator functioning as a scaffold in membrane-anchoring of Rag GTPases and mTORC1
title_full	Structural basis for Ragulator functioning as a scaffold in membrane-anchoring of Rag GTPases and mTORC1
title_fullStr	Structural basis for Ragulator functioning as a scaffold in membrane-anchoring of Rag GTPases and mTORC1
title_full_unstemmed	Structural basis for Ragulator functioning as a scaffold in membrane-anchoring of Rag GTPases and mTORC1
title_sort	structural basis for ragulator functioning as a scaffold in membrane-anchoring of rag gtpases and mtorc1
publisher	Nature Publishing Group
series	Nature Communications
issn	2041-1723
publishDate	2017-11-01
description	Activated Rag GTPases recruit mTORC1 to lysosomes. Here the authors present the crystal structure of the Ragulator complex and identify the binding sites for the Roadblock domains of Rag GTPases, which gives insights how Rag GTPases are tethered to the lysosomal membrane.
url	https://doi.org/10.1038/s41467-017-01567-4
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Structural basis for Ragulator functioning as a scaffold in membrane-anchoring of Rag GTPases and mTORC1

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