Oligomerization and phosphorylation dependent regulation of ArgBP2 adaptive capabilities and associated functions.

ArgBP2 (Arg-Binding Protein 2/SORBS2) is an adaptor protein involved in cytoskeleton associated signal transduction, thereby regulating cell migration and adhesion. These features are associated with its antitumoral role in pancreatic cancer cells. Tyrosine phosphorylation of ArgBP2, mediated by c-A...

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Autores principales:	Julie Roignot, Thomas Bonacci, Eric Ghigo, Juan L Iovanna, Philippe Soubeyran
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2014
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/ea790c81625e4ac798f7b01a39f89572
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spelling	oai:doaj.org-article:ea790c81625e4ac798f7b01a39f895722021-11-18T08:35:35ZOligomerization and phosphorylation dependent regulation of ArgBP2 adaptive capabilities and associated functions.1932-620310.1371/journal.pone.0087130https://doaj.org/article/ea790c81625e4ac798f7b01a39f895722014-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/24475245/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203ArgBP2 (Arg-Binding Protein 2/SORBS2) is an adaptor protein involved in cytoskeleton associated signal transduction, thereby regulating cell migration and adhesion. These features are associated with its antitumoral role in pancreatic cancer cells. Tyrosine phosphorylation of ArgBP2, mediated by c-Abl kinase and counterbalanced by PTP-PEST phosphatase, regulates many of its interactions. However, the exact mechanisms of action and of regulation of ArgBP2 remain largely unknown. We found that ArgBP2 has the capacity to form oligomers which are destabilized by tyrosine phosphorylation. We could show that ArgBP2 oligomerization involves the binding of one of its SH3 domains to a specific proline rich cluster. ArgBP2 self-association increases its binding to some of its molecular partners and decreased its affinity for others. Hence, the phosphorylation/oligomerization state of ArgBP2 directly regulates its functions by modulating its adaptive capabilities. Importantly, using a human pancreatic cancer cell model (MiaPaCa-2 cells), we could validate that this property of ArgBP2 is critical for its cytoskeleton associated functions. In conclusions, we describe a new mechanism of regulation of ArgBP2 where tyrosine phosphorylation of the protein interfere with a SH3 mediated self-interaction, thereby controlling its panel of interacting partners and related functions.Julie RoignotThomas BonacciEric GhigoJuan L IovannaPhilippe SoubeyranPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 9, Iss 1, p e87130 (2014)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Julie Roignot Thomas Bonacci Eric Ghigo Juan L Iovanna Philippe Soubeyran Oligomerization and phosphorylation dependent regulation of ArgBP2 adaptive capabilities and associated functions.
description	ArgBP2 (Arg-Binding Protein 2/SORBS2) is an adaptor protein involved in cytoskeleton associated signal transduction, thereby regulating cell migration and adhesion. These features are associated with its antitumoral role in pancreatic cancer cells. Tyrosine phosphorylation of ArgBP2, mediated by c-Abl kinase and counterbalanced by PTP-PEST phosphatase, regulates many of its interactions. However, the exact mechanisms of action and of regulation of ArgBP2 remain largely unknown. We found that ArgBP2 has the capacity to form oligomers which are destabilized by tyrosine phosphorylation. We could show that ArgBP2 oligomerization involves the binding of one of its SH3 domains to a specific proline rich cluster. ArgBP2 self-association increases its binding to some of its molecular partners and decreased its affinity for others. Hence, the phosphorylation/oligomerization state of ArgBP2 directly regulates its functions by modulating its adaptive capabilities. Importantly, using a human pancreatic cancer cell model (MiaPaCa-2 cells), we could validate that this property of ArgBP2 is critical for its cytoskeleton associated functions. In conclusions, we describe a new mechanism of regulation of ArgBP2 where tyrosine phosphorylation of the protein interfere with a SH3 mediated self-interaction, thereby controlling its panel of interacting partners and related functions.
format	article
author	Julie Roignot Thomas Bonacci Eric Ghigo Juan L Iovanna Philippe Soubeyran
author_facet	Julie Roignot Thomas Bonacci Eric Ghigo Juan L Iovanna Philippe Soubeyran
author_sort	Julie Roignot
title	Oligomerization and phosphorylation dependent regulation of ArgBP2 adaptive capabilities and associated functions.
title_short	Oligomerization and phosphorylation dependent regulation of ArgBP2 adaptive capabilities and associated functions.
title_full	Oligomerization and phosphorylation dependent regulation of ArgBP2 adaptive capabilities and associated functions.
title_fullStr	Oligomerization and phosphorylation dependent regulation of ArgBP2 adaptive capabilities and associated functions.
title_full_unstemmed	Oligomerization and phosphorylation dependent regulation of ArgBP2 adaptive capabilities and associated functions.
title_sort	oligomerization and phosphorylation dependent regulation of argbp2 adaptive capabilities and associated functions.
publisher	Public Library of Science (PLoS)
publishDate	2014
url	https://doaj.org/article/ea790c81625e4ac798f7b01a39f89572
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Oligomerization and phosphorylation dependent regulation of ArgBP2 adaptive capabilities and associated functions.

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