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Se oferta un Contrato Postdoctoral con cargo a la Red Temática de Investigación de Centros de Cáncer (RTICC). 2007-2010 (33.000 € brutos/año). Tema de trabajo: Regulación espacio-temporal de las señales Ras–ERK. Requisitos básicos: Experiencia en biología molecular (vectores de expresión, cloning, PCR, mutagénesis, etc) y en biología celular (cultivos celulares, immunoflouerescencia, etc). Se valorará experiencia en señalización y, particularmente, en trabajo con ratones manipulados genéticamente. Interesados ponerse en contacto con el Dr. Piero Crespo en: Unidad de Biomedicina, Instituto de Investigaciones Biomédicas, CSIC -Universidad de Cantabria. Departamento de Biología Molecular, Facultad de Medicina. C/ Cardenal Herrera Oria s/n. Santander 39011. Tl: 34-942-200959. e-mail: crespop@rticcc.com
PUBLICACIONES SCI DEL GRUPO EN LOS ÚLTIMOS CINCO AÑOS
1. Esparís-Ogando A. et al. “ERK5 participates in neuregulin signal transduction and is constitutively active in breast cancer cells overexpressing ErbB2.” Mol. Cell. Biol., 22, 270-285. (2002).
2. Matallanas D., et al. “Differences in the inhibitory specificities of H-Ras, K-Ras and N-Ras (N17) dominant negative mutants are related to their membrane microlocalization”. J. Biol. Chem., 278, 4572-4581. (2003).
3. Sanz-Moreno et al. “p38a isoform Mxi2 binds to ERK1/2 Mitogen-activated protein kinase and regulates its nuclear activity by sustaining its phosphorylation levels”. Mol. Cell. Biol., 23, 3079-3090. (2003).
- Caloca M.J., et al “The Vav/Rac route positively regulates Ras signaling by direct activation of the Ras guanosine nucleotide exchange factor CalDag/Ras GRP”. EMBO J., 22, 3326-3336. (2003).
5. Vargiu P.F., et al., "The small GTP-binding protein, Rhes regulates signal transduction from G protein-coupled receptors". Oncogene. 23, 559-568. (2004).
6. Arozarena I., et al “Activation of H-Ras in the endoplasmic reticulum by the Ras-GRF family guanine nucleotide exchange factors”. Mol. Cell. Biol., 24, 1516-1530. (2004).
7. Ajenjo N., et al. “Subcellular localization determines the protective effect of activated ERK2 against distinct apoptogenic stimuli in myeloid leukemia cells”. J. Biol. Chem., 279, 32813-32823. (2004).
8. Vaqué J.P., et al. “Myc antagonizes Ras-mediated growth arrest in myeloid leukemia cells through the inhibition of the Raf-ERK-p21 pathway”. J. Biol. Chem., 280, 1112-1122. (2005).
9. Matallanas D., et al. “Distinct utilization of effectors and biological outcomes resulting from site-specific Ras activation: Ras functions in lipid rafts and Golgi complex are dispensable for proliferation and transformation”. Mol. Cell. Biol., 26, 100-116. (2006).
10. Peregrín S., et al. “Phosphorylation of p38 by GRK2 at the docking groove unveils a novel mechanism for inactivating p38 MAPK”. Curr. Biol., 16, 2042-2047. (2006).
11. Casar B., et al. “Mxi2 promotes stimulus-independent ERKs nuclear translocation”. EMBO J., 26, 635-646. (2007).
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