Education

Ph.D in Molecular Biology, Department of Molecular Biology, University of Cantabria (SPAIN), 1991

Current position

Assistant Professor, Instituto de Biomedicina y Biotecnología de Cantabria (IBBTEC) , Consejo Superior de Investigaciones Científicas (CSIC)

Publications

1. Casar, B. and Crespo, P. (2016). ERK Signals: Scaffolding Scaffolds? Front Cell Dev Biol 4: 49.

2. Herrero, A., Casar, B., Colon-Bolea, P., Agudo-Ibanez, L. and Crespo, P. (2016). Defined spatiotemporal features of RAS-ERK signals dictate cell fate in MCF-7 mammary epithelial cells. Mol Biol Cell 27(12): 1958-1968.

3. Herrero, A., Pinto, A., Colon-Bolea, P., Casar, B., Jones, M., Agudo-Ibanez, L., Vidal, R., Tenbaum, S. P., Nuciforo, P., Valdizan, E. M., Horvath, Z., Orfi, L., Pineda-Lucena, A., Bony, E., Keri, G., Rivas, G., Pazos, A., Gozalbes, R., Palmer, H. G., Hurlstone, A. and Crespo, P. (2015). Small Molecule Inhibition of ERK Dimerization Prevents Tumorigenesis by RAS-ERK Pathway Oncogenes. Cancer Cell 28(2): 170-182.

4. Hooper, J., Yaowu, H., Casar, B., Ying, D., Wortmann, A., Adams, M., Clements, J., Quigley, J. (2013). Novel protease mediated mechanisms promote the spread of cancer cells via the blood circulation. Faseb Journal.

5. Zajac, E., Casar, B., Scweighofer, B., Kupriyanova, T., Rimann, I., Deryugina, E., Junckenr-Jensen, A. and Quigley, J. (2013). Abstract PR10: High angiogenic capacity of inflammatory neutrophils and polarized M2 macrophages is determined byproduction of MMP-9 unencumbered by its natural inhibitor TIMP-1. Cancer research.

6. Hooper, J., Yaowu, H., Wortmann, A., Casar, B., Adams, M. and Quigley, J. (2013). A novel and inhibitable pro-metastatic mechanism in prostate cancer. Bju International. 112, pp. 43-44.

7. Juncker Jensen, A., Casar, B., Rimann, I., Zajac, E., Kupriyanova, T., Deryugina, E. and Quigley, J. (2013). Abstract C18: Matrix metalloproteinase-1 (MMP-1) facilitates intravasation and vascular dissemination of human carcinoma cells by regulating the microarchitecture and permeability of intratumoral vasculature. Cancer research C-18.

8. Casar, B., Rimann, I., Kato, H., Shattil, S. J., Quigley, J. P. and Deryugina, E. I. (2014). In vivo cleaved CDCP1 promotes early tumor dissemination via complexing with activated beta1 integrin and induction of FAK/PI3K/Akt motility signaling. Oncogene 33(2): 255-268.

9. Casar, B., Hooper, J. D., Quigley, J. P. and Deryugina, E. I. (2012). Blocking of CDCP1 In Vivo Cleavage Presents Akt-Dependent Survival of Cancer Cells and Inhibits Their Metastatic Colonization via PARP1-Mediated Apoptosis. Faseb Journal.

10. Casar, B., He, Y., Iconomou, M., Hooper, J. D., Quigley, J. P. and Deryugina, E. I. (2012). Blocking of CDCP1 cleavage in vivo prevents Akt-dependent survival and inhibits metastatic colonization through PARP1-mediated apoptosis of cancer cells. Oncogene 31(35): 3924-3938.

11. Casar, B., Rodriguez, J., Gibor, G., Seger, R. and Crespo, P. (2012). Mxi2 sustains ERK1/2 phosphorylation in the nucleus by preventing ERK1/2 binding to phosphatases. Biochem J 441(2): 571-578.

12. Zajac, E., Schweighofer, B., Kupriyanova, T., Casar, B., Rimann, I., Juncker-Jensen, A., Deryugina, E. and Quigley, J. P. (2012). Pro-Angiogenic Capacity of MMP-9 Produced by Different Types of InflammatoryLeukocytes is Determined by the Levels of TIMP-1 Complexed with the MMP-9 Proenzyme. Faseb Journal.

13. Rodriguez, J., Calvo, F., Gonzalez, J. M., Casar, B., Andres, V. and Crespo, P. (2010). ERK1/2 MAP kinases promote cell cycle entry by rapid, kinase-independent disruption of retinoblastoma-lamin A complexes. J Cell Biol 191(5): 967-979.

14. Casar, B., Pinto, A. and Crespo, P. (2009). ERK dimers and scaffold proteins: unexpected partners for a forgotten (cytoplasmic) task. Cell Cycle 8(7): 1007-1013.

15. Casar, B., Arozarena, I., Sanz-Moreno, V., Pinto, A., Agudo-Ibanez, L., Marais, R., Lewis, R. E., Berciano, M. T. and Crespo, P. (2009). Ras subcellular localization defines extracellular signal-regulated kinase 1 and 2 substrate specificity through distinct utilization of scaffold proteins. Mol Cell Biol 29(5): 1338-1353.

16. Casar, B., Pinto, A. and Crespo, P. (2008). Essential role of ERK dimers in the activation of cytoplasmic but not nuclear substrates by ERK-scaffold complexes. Mol Cell 31(5): 708-721.

17. Gonzalez, J. M., Navarro-Puche, A., Casar, B., Crespo, P. and Andres, V. (2008). Fast regulation of AP-1 activity through interaction of lamin A/C, ERK1/2, and c-Fos at the nuclear envelope. J Cell Biol 183(4): 653-666.

18. Casar, B., Sanz-Moreno, V., Yazicioglu, M. N., Rodriguez, J., Berciano, M. T., Lafarga, M., Cobb, M. H. and Crespo, P. (2007). Mxi2 promotes stimulus-independent ERK nuclear translocation. EMBO J 26(3): 635-646.

19. Sanz-Moreno, V., Casar, B. and Crespo, P. (2003). p38alpha isoform Mxi2 binds to extracellular signal-regulated kinase 1 and 2 mitogen-activated protein kinase and regulates its nuclear activity by sustaining its phosphorylation levels. Mol Cell Biol 23(9): 3079-3090.