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Binding of PTEN to specific PDZ domains contributes to PTEN protein stability and phosphorylation by microtubule-associated serine/threonine kinases

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Binding of PTEN to specific PDZ domains contributes to PTEN protein stability and phosphorylation by microtubule-associated serine/threonine kinases

dc.contributor.author	Valiente, Miguel
dc.contributor.author	Andrés-Pons, Amparo
dc.contributor.author	Gomar, Beatriz
dc.contributor.author	Torres Ibáñez, José Manuel
dc.contributor.author	Gil, Anabel
dc.contributor.author	Tapparel, Caroline
dc.contributor.author	Antonarakis, Stylianos E.
dc.contributor.author	Pulido Murillo, Rafael
dc.date.accessioned	2022-10-20T16:56:02Z
dc.date.available	2022-10-20T16:56:02Z
dc.date.issued	2005
dc.identifier.citation	Valiente, Miguel Andrés-Pons, Amparo Gomar, Beatriz Torres Ibáñez, José Manuel Gil, Anabel Tapparel, Caroline Antonarakis, Stylianos E. Pulido Murillo, Rafael 2005 Binding of PTEN to specific PDZ domains contributes to PTEN protein stability and phosphorylation by microtubule-associated serine/threonine kinases Journal of Biological Chemistry 280 32 28936 28943
dc.identifier.uri	https://hdl.handle.net/10550/84228
dc.description.abstract	The tumor suppressor phosphatase PTEN is a key regulator of cell growth and apoptosis that interacts with PDZ domains from regulatory proteins, including MAGI-1/2/3, hDlg, and MAST205. Here we identified novel PTEN-binding PDZ domains within the MAST205-related proteins, syntrophin-associated serine/threonine kinase and MAST3, characterized the regions of PTEN involved in its interaction with distinctive PDZ domains, and analyzed the functional consequences on PTEN of PDZ domain binding. Using a panel of PTEN mutations, as well as PTEN chimeras containing distinct domains of the related protein TPTE, we found that the PTP and C2 domains of PTEN do not affect PDZ domain binding and that the C-terminal tail of PTEN (residues 350-403) provides selectivity to recognize specific PDZ domains from MAGI-2, hDlg, and MAST205. Binding of PTEN to the PDZ-2 domain from MAGI-2 increased PTEN protein stability. Furthermore, binding of PTEN to the PDZ domains from microtubule-associated serine/threonine kinases facilitated PTEN phosphorylation at its C terminus by these kinases. Our results suggest an important role for the C-terminal region of PTEN in the selective association with scaffolding and/or regulatory molecules and provide evidence that PDZ domain binding stabilizes PTEN and targets this tumor suppressor for phosphorylation by microtubule-associated serine/threonine kinases.
dc.language.iso	eng
dc.relation.ispartof	Journal of Biological Chemistry, 2005, vol. 280, num. 32, p. 28936-28943
dc.subject	Proteïnes supressores de tumors
dc.subject	Cèl·lules
dc.title	Binding of PTEN to specific PDZ domains contributes to PTEN protein stability and phosphorylation by microtubule-associated serine/threonine kinases
dc.type	journal article	es_ES
dc.date.updated	2022-10-20T16:56:02Z
dc.identifier.doi	10.1074/jbc.M504761200
dc.identifier.idgrec	080769
dc.rights.accessRights	open access	es_ES