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dc.contributor.author | Blanco-Aparicio, Carmen | |
dc.contributor.author | Torres Ibáñez, José Manuel | |
dc.contributor.author | Pulido Murillo, Rafael | |
dc.date.accessioned | 2022-11-03T14:27:04Z | |
dc.date.available | 2022-11-03T14:27:04Z | |
dc.date.issued | 1999 | |
dc.identifier.citation | Blanco-Aparicio, Carmen Torres Ibáñez, José Manuel Pulido Murillo, Rafael 1999 A novel regulatory mechanism of MAP kinases activation and nuclear translocation mediated by PKA and the PTP-SL tyrosine phosphatase Journal of Cell Biology 147 6 1129 1136 | |
dc.identifier.uri | https://hdl.handle.net/10550/84390 | |
dc.description.abstract | Protein tyrosine phosphatase PTP-SL retains mitogen-activated protein (MAP) kinases in the cytoplasm in an inactive form by association through a kinase interaction motif (KIM) and tyrosine dephosphorylation. The related tyrosine phosphatases PTP-SL and STEP were phosphorylated by the cAMP-dependent protein kinase A (PKA). The PKA phosphorylation site on PTP-SL was identified as the Ser231 residue, located within the KIM. Upon phosphorylation of Ser231, PTP-SL binding and tyrosine dephosphorylation of the MAP kinases extracellular signal-regulated kinase (ERK)1/2 and p38α were impaired. Furthermore, treatment of COS-7 cells with PKA activators, or overexpression of the Cα catalytic subunit of PKA, inhibited the cytoplasmic retention of ERK2 and p38α by wild-type PTP-SL, but not by a PTP-SL S231A mutant. These findings support the existence of a novel mechanism by which PKA may regulate the activation and translocation to the nucleus of MAP kinases. | |
dc.language.iso | eng | |
dc.relation.ispartof | Journal of Cell Biology, 1999, vol. 147, num. 6, p. 1129-1136 | |
dc.subject | Cèl·lules | |
dc.subject | Enzims | |
dc.title | A novel regulatory mechanism of MAP kinases activation and nuclear translocation mediated by PKA and the PTP-SL tyrosine phosphatase | |
dc.type | journal article | es_ES |
dc.date.updated | 2022-11-03T14:27:04Z | |
dc.identifier.doi | 10.1083/jcb.147.6.1129 | |
dc.identifier.idgrec | 080762 | |
dc.rights.accessRights | open access | es_ES |