Structural basis of liprin-α-promoted LAR-RPTP clustering for modulation of phosphatase activity

Leukocyte common antigen-related receptor protein tyrosine phosphatases (LAR-RPTPs) mediate guided axon growth and synapse formation and liprin-α proteins are their intracellular binding partners. Here the authors present the crystal structure of the phosphatase domains from the LAR-RPTP family memb...

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Autores principales:	Xingqiao Xie, Ling Luo, Mingfu Liang, Wenchao Zhang, Ting Zhang, Cong Yu, Zhiyi Wei
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/b7627407bf5a414782b084a50ea87bfd
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spelling	oai:doaj.org-article:b7627407bf5a414782b084a50ea87bfd2021-12-02T17:32:26ZStructural basis of liprin-α-promoted LAR-RPTP clustering for modulation of phosphatase activity10.1038/s41467-019-13949-x2041-1723https://doaj.org/article/b7627407bf5a414782b084a50ea87bfd2020-01-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-13949-xhttps://doaj.org/toc/2041-1723Leukocyte common antigen-related receptor protein tyrosine phosphatases (LAR-RPTPs) mediate guided axon growth and synapse formation and liprin-α proteins are their intracellular binding partners. Here the authors present the crystal structure of the phosphatase domains from the LAR-RPTP family member LAR bound to the SAM repeats of liprin-α3 and show that liprin-α binding enhances LAR cluster formation and reduces LAR phosphatase activity in cells.Xingqiao XieLing LuoMingfu LiangWenchao ZhangTing ZhangCong YuZhiyi WeiNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-12 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Xingqiao Xie Ling Luo Mingfu Liang Wenchao Zhang Ting Zhang Cong Yu Zhiyi Wei Structural basis of liprin-α-promoted LAR-RPTP clustering for modulation of phosphatase activity
description	Leukocyte common antigen-related receptor protein tyrosine phosphatases (LAR-RPTPs) mediate guided axon growth and synapse formation and liprin-α proteins are their intracellular binding partners. Here the authors present the crystal structure of the phosphatase domains from the LAR-RPTP family member LAR bound to the SAM repeats of liprin-α3 and show that liprin-α binding enhances LAR cluster formation and reduces LAR phosphatase activity in cells.
format	article
author	Xingqiao Xie Ling Luo Mingfu Liang Wenchao Zhang Ting Zhang Cong Yu Zhiyi Wei
author_facet	Xingqiao Xie Ling Luo Mingfu Liang Wenchao Zhang Ting Zhang Cong Yu Zhiyi Wei
author_sort	Xingqiao Xie
title	Structural basis of liprin-α-promoted LAR-RPTP clustering for modulation of phosphatase activity
title_short	Structural basis of liprin-α-promoted LAR-RPTP clustering for modulation of phosphatase activity
title_full	Structural basis of liprin-α-promoted LAR-RPTP clustering for modulation of phosphatase activity
title_fullStr	Structural basis of liprin-α-promoted LAR-RPTP clustering for modulation of phosphatase activity
title_full_unstemmed	Structural basis of liprin-α-promoted LAR-RPTP clustering for modulation of phosphatase activity
title_sort	structural basis of liprin-α-promoted lar-rptp clustering for modulation of phosphatase activity
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/b7627407bf5a414782b084a50ea87bfd
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Structural basis of liprin-α-promoted LAR-RPTP clustering for modulation of phosphatase activity

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