Phosphorylation of Rab-coupling protein by LMTK3 controls Rab14-dependent EphA2 trafficking to promote cell:cell repulsion

Ephrin receptors mediate contact inhibition, but their intracellular trafficking during this process is unknown. Here the authors show that EphA2 receptor trafficking is regulated by the Rab GTPase effector Rab-coupling protein, which associates with Rab14-endosomes upon LMTK3-mediated phosphorylati...

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Autores principales: Christine Gundry, Sergi Marco, Elena Rainero, Bryan Miller, Emmanuel Dornier, Louise Mitchell, Patrick T. Caswell, Andrew D. Campbell, Anna Hogeweg, Owen J. Sansom, Jennifer P. Morton, Jim C. Norman
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Publicado: Nature Portfolio 2017
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Acceso en línea:https://doaj.org/article/74f2ebe037a54017b8f114ad988e154b
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spelling oai:doaj.org-article:74f2ebe037a54017b8f114ad988e154b2021-12-02T15:38:51ZPhosphorylation of Rab-coupling protein by LMTK3 controls Rab14-dependent EphA2 trafficking to promote cell:cell repulsion10.1038/ncomms146462041-1723https://doaj.org/article/74f2ebe037a54017b8f114ad988e154b2017-03-01T00:00:00Zhttps://doi.org/10.1038/ncomms14646https://doaj.org/toc/2041-1723Ephrin receptors mediate contact inhibition, but their intracellular trafficking during this process is unknown. Here the authors show that EphA2 receptor trafficking is regulated by the Rab GTPase effector Rab-coupling protein, which associates with Rab14-endosomes upon LMTK3-mediated phosphorylation.Christine GundrySergi MarcoElena RaineroBryan MillerEmmanuel DornierLouise MitchellPatrick T. CaswellAndrew D. CampbellAnna HogewegOwen J. SansomJennifer P. MortonJim C. NormanNature PortfolioarticleScienceQENNature Communications, Vol 8, Iss 1, Pp 1-15 (2017)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Christine Gundry
Sergi Marco
Elena Rainero
Bryan Miller
Emmanuel Dornier
Louise Mitchell
Patrick T. Caswell
Andrew D. Campbell
Anna Hogeweg
Owen J. Sansom
Jennifer P. Morton
Jim C. Norman
Phosphorylation of Rab-coupling protein by LMTK3 controls Rab14-dependent EphA2 trafficking to promote cell:cell repulsion
description Ephrin receptors mediate contact inhibition, but their intracellular trafficking during this process is unknown. Here the authors show that EphA2 receptor trafficking is regulated by the Rab GTPase effector Rab-coupling protein, which associates with Rab14-endosomes upon LMTK3-mediated phosphorylation.
format article
author Christine Gundry
Sergi Marco
Elena Rainero
Bryan Miller
Emmanuel Dornier
Louise Mitchell
Patrick T. Caswell
Andrew D. Campbell
Anna Hogeweg
Owen J. Sansom
Jennifer P. Morton
Jim C. Norman
author_facet Christine Gundry
Sergi Marco
Elena Rainero
Bryan Miller
Emmanuel Dornier
Louise Mitchell
Patrick T. Caswell
Andrew D. Campbell
Anna Hogeweg
Owen J. Sansom
Jennifer P. Morton
Jim C. Norman
author_sort Christine Gundry
title Phosphorylation of Rab-coupling protein by LMTK3 controls Rab14-dependent EphA2 trafficking to promote cell:cell repulsion
title_short Phosphorylation of Rab-coupling protein by LMTK3 controls Rab14-dependent EphA2 trafficking to promote cell:cell repulsion
title_full Phosphorylation of Rab-coupling protein by LMTK3 controls Rab14-dependent EphA2 trafficking to promote cell:cell repulsion
title_fullStr Phosphorylation of Rab-coupling protein by LMTK3 controls Rab14-dependent EphA2 trafficking to promote cell:cell repulsion
title_full_unstemmed Phosphorylation of Rab-coupling protein by LMTK3 controls Rab14-dependent EphA2 trafficking to promote cell:cell repulsion
title_sort phosphorylation of rab-coupling protein by lmtk3 controls rab14-dependent epha2 trafficking to promote cell:cell repulsion
publisher Nature Portfolio
publishDate 2017
url https://doaj.org/article/74f2ebe037a54017b8f114ad988e154b
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