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Interaction of Mitogen-activated Protein Kinases with the Kinase Interaction Motif of the Tyrosine Phosphatase PTP-SL Provides Substrate Specificity and Retains ERK2 in the Cytoplasm

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Interaction of Mitogen-activated Protein Kinases with the Kinase Interaction Motif of the Tyrosine Phosphatase PTP-SL Provides Substrate Specificity and Retains ERK2 in the Cytoplasm

dc.contributor.author	Zúñiga, Ángel
dc.contributor.author	Torres Ibáñez, José Manuel
dc.contributor.author	Úbeda, Josefa
dc.contributor.author	Pulido Murillo, Rafael
dc.date.accessioned	2022-10-21T13:46:27Z
dc.date.available	2022-10-21T13:46:27Z
dc.date.issued	1999
dc.identifier.citation	Zúñiga, Ángel Torres Ibáñez, José Manuel Úbeda, Josefa Pulido Murillo, Rafael 1999 Interaction of Mitogen-activated Protein Kinases with the Kinase Interaction Motif of the Tyrosine Phosphatase PTP-SL Provides Substrate Specificity and Retains ERK2 in the Cytoplasm Journal of Biological Chemistry 274 31 21900 21907
dc.identifier.uri	https://hdl.handle.net/10550/84237
dc.description.abstract	ERK1 and ERK2 associate with the tyrosine phosphatase PTP-SL through a kinase interaction motif (KIM) located in the juxtamembrane region of PTP-SL. A glutathioneS-transferase (GST)-PTP-SL fusion protein containing the KIM associated with ERK1 and ERK2 as well as with p38/HOG, but not with the related JNK1 kinase or with protein kinase A or C. Accordingly, ERK2 showed in vitro substrate specificity to phosphorylate GST-PTP-SL in comparison with GST-c-Jun. Furthermore, tyrosine dephosphorylation of ERK2 by the PTP-SLΔKIM mutant was impaired. Thein vitro association of ERK1/2 with GST-PTP-SL was highly stable; however, low concentrations of nucleotides partially dissociated the ERK1/2·PTP-SL complex. Partial deletions of the KIM abrogated the association of PTP-SL with ERK1/2, indicating that KIM integrity is required for interaction. Amino acid substitution analysis revealed that Arg and Leu residues within the KIM are essential for the interaction and suggested a regulatory role for Ser231. Finally, coexpression of PTP-SL and ERK2 in COS-7 cells resulted in the retention of ERK2 in the cytoplasm in a KIM-dependent manner. Our results demonstrate that the noncatalytic region of PTP-SL associates with mitogen-activated protein kinases with high affinity and specificity, providing a mechanism for substrate specificity, and suggest a role for PTP-SL in the regulation of mitogen-activated protein kinase translocation to the nucleus upon activation.
dc.language.iso	eng
dc.relation.ispartof	Journal of Biological Chemistry, 1999, vol. 274, num. 31, p. 21900-21907
dc.subject	Cèl·lules
dc.subject	Proteïnes
dc.title	Interaction of Mitogen-activated Protein Kinases with the Kinase Interaction Motif of the Tyrosine Phosphatase PTP-SL Provides Substrate Specificity and Retains ERK2 in the Cytoplasm
dc.type	journal article	es_ES
dc.date.updated	2022-10-21T13:46:28Z
dc.identifier.doi	10.1074/jbc.274.31.21900
dc.identifier.idgrec	080761
dc.rights.accessRights	open access	es_ES