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Campo DC | Valor | Lengua/Idioma |
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dc.contributor.author | Arévalo, Juan Carlos | - |
dc.contributor.author | Chao, Moses V. | - |
dc.contributor.author | Martín-Zanca, Dionisio | - |
dc.contributor.author | Pérez González, Pilar | - |
dc.date.accessioned | 2013-02-04T09:10:05Z | - |
dc.date.available | 2013-02-04T09:10:05Z | - |
dc.date.issued | 2001 | - |
dc.identifier | doi: 10.1038/sj.onc.1204215 | - |
dc.identifier | issn: 0950-9232 | - |
dc.identifier | e-issn: 1476-5594 | - |
dc.identifier.citation | Oncogene 20(10): 1229-1234 (2001) | - |
dc.identifier.uri | http://hdl.handle.net/10261/65750 | - |
dc.description.abstract | The TrkA NGF receptor extracellular region contains three leucine repeats flanked by cysteine clusters and two immunoglobulin-like domains that are required for specific ligand binding. Deletion of the immunoglobulin-like domains abolishes NGF binding and causes ligand independent activation of the receptor. Here we report a specific mutation that increases the binding affinity of the TrkA receptor for NGF. A change of proline 203 to alanine (P203A) in the linker region between the leucine repeats and the first Ig-like domain increased NGF binding by decreasing the ligand rate of dissociation. This mutated receptor was appropriately expressed on the cell surface and promoted ligand-independent neurite outgrowth in PC12nnr5 cells. The mutant receptor was capable of spontaneous dimerization and was constitutively phosphorylated in the absence of ligand. Moreover, expression of TrkA-P203A receptor in fibroblasts induced DNA synthesis and transformation and generated turnouts in nude mice. These data suggest that domains outside of the immunoglobulin-like structure contribute to ligand binding and constitutive activation of Trk receptors. | - |
dc.description.sponsorship | This work was supported by grants from the Fundacion Ramon Areces and the European Union Program BIO4- CT96-0285. JC Arevalo was a recipient of fellowships from those grants. Grant support for MV Chao and BL Hempstead were from the NIH. | - |
dc.language.iso | eng | - |
dc.publisher | Nature Publishing Group | - |
dc.rights | closedAccess | - |
dc.title | A novel mutation within the extracellular domain of TrkA causes constitutive receptor activation | - |
dc.type | artículo | - |
dc.identifier.doi | 10.1038/sj.onc.1204215 | - |
dc.date.updated | 2013-02-04T09:10:06Z | - |
dc.description.version | Peer Reviewed | - |
dc.type.coar | http://purl.org/coar/resource_type/c_6501 | es_ES |
item.fulltext | No Fulltext | - |
item.languageiso639-1 | en | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.openairetype | artículo | - |
item.cerifentitytype | Publications | - |
item.grantfulltext | none | - |
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