| http://purl.uniprot.org/citations/19948721 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/19948721 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/19948721 | http://www.w3.org/2000/01/rdf-schema#comment | "Nitric oxide (NO) plays a pivotal role in tumorigenesis, particularly with relation to cancer cell invasion and metastasis. NO can reversibly couple to cysteine thiols to form an S-nitrosothiol, which regulates the enzymatic activities of target proteins. c-Src is a tyrosine kinase that promotes cancer cell invasion and metastasis. Interestingly, c-Src can be activated by NO stimulation. However, mechanisms by which NO stimulates Src kinase activity have not been elucidated. We report here that NO causes S-nitrosylation of c-Src at cysteine 498 (Cys(498)) to stimulate its kinase activity. Cys(498) is conserved among Src family kinases, and Cys(506) of c-Yes, which corresponds to Cys(498) of c-Src, was also important for the NO-mediated activation of c-Yes. Estrogens may work synergistically with NO to induce the proliferation and migration of many kinds of breast cancer cells. For example, beta-estradiol induces the expression of endothelial nitric synthase and production of NO in MCF7 cells. We found that activation of c-Src in MCF7 cells by beta-estradiol stimulation was mediated by the S-nitrosylation of Cys(498). In addition, we report that disruption of E-cadherin junctions and enhancement of cell invasion by beta-estradiol stimulation was mediated by NO-dependent activation of c-Src. These results identify a novel signaling pathway that links NO and Src family kinases to cancer cell invasion and metastasis."xsd:string |
| http://purl.uniprot.org/citations/19948721 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m109.059782"xsd:string |
| http://purl.uniprot.org/citations/19948721 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m109.059782"xsd:string |
| http://purl.uniprot.org/citations/19948721 | http://purl.uniprot.org/core/author | "Ito S."xsd:string |
| http://purl.uniprot.org/citations/19948721 | http://purl.uniprot.org/core/author | "Ito S."xsd:string |
| http://purl.uniprot.org/citations/19948721 | http://purl.uniprot.org/core/author | "Rahman M.A."xsd:string |
| http://purl.uniprot.org/citations/19948721 | http://purl.uniprot.org/core/author | "Rahman M.A."xsd:string |
| http://purl.uniprot.org/citations/19948721 | http://purl.uniprot.org/core/author | "Hasegawa H."xsd:string |
| http://purl.uniprot.org/citations/19948721 | http://purl.uniprot.org/core/author | "Hasegawa H."xsd:string |
| http://purl.uniprot.org/citations/19948721 | http://purl.uniprot.org/core/author | "Hamaguchi M."xsd:string |
| http://purl.uniprot.org/citations/19948721 | http://purl.uniprot.org/core/author | "Hamaguchi M."xsd:string |
| http://purl.uniprot.org/citations/19948721 | http://purl.uniprot.org/core/author | "Hyodo T."xsd:string |
| http://purl.uniprot.org/citations/19948721 | http://purl.uniprot.org/core/author | "Hyodo T."xsd:string |
| http://purl.uniprot.org/citations/19948721 | http://purl.uniprot.org/core/author | "Senga T."xsd:string |
| http://purl.uniprot.org/citations/19948721 | http://purl.uniprot.org/core/author | "Senga T."xsd:string |
| http://purl.uniprot.org/citations/19948721 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
| http://purl.uniprot.org/citations/19948721 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
| http://purl.uniprot.org/citations/19948721 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/19948721 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/19948721 | http://purl.uniprot.org/core/pages | "3806-3814"xsd:string |
| http://purl.uniprot.org/citations/19948721 | http://purl.uniprot.org/core/pages | "3806-3814"xsd:string |
| http://purl.uniprot.org/citations/19948721 | http://purl.uniprot.org/core/title | "S-nitrosylation at cysteine 498 of c-Src tyrosine kinase regulates nitric oxide-mediated cell invasion."xsd:string |
| http://purl.uniprot.org/citations/19948721 | http://purl.uniprot.org/core/title | "S-nitrosylation at cysteine 498 of c-Src tyrosine kinase regulates nitric oxide-mediated cell invasion."xsd:string |