
Department of Neuroscience, Cell Biology, & Anatomy
2.104C Medical Research Building (MRB)
Route: 1069 |
Tel: (409) 772-5480 |
Fax: (409) 772-3222 |
jnavarro@utmb.eduEducation and Training
PhD in Physiology, Boston University School of Medicine, Boston, MA
MS in Pharmacology, Worcester Foundation for Experimental Biology,
Shrewsbury, MA and Universidad Peruana Cayetano Heredia, Lima, Peru
Post-Doctoral in Biochemistry, Cornell University, Ithaca, NY
BS in Biology, Universidad Peruana Cayetano Heredia, Lima, Peru
Research Interests
Our work focuses on elucidating the molecular mechanisms of G
protein-coupled receptors. These are seven-helix transmembrane
receptors acting as detectors of signals including odor, light,
hormones, neurotransmitters, and as mediators for the entry of HIV-1.
Genes encoding these receptors occupy a hefty 3% of the human genome.
Of importance is that these receptors are the target of about 60% of
drugs used to treat human diseases. In my laboratory we are applying
X-ray crystallography to elucidate the atomic structure of seven-helix
transmembrane receptors. Genetic and biophysical approaches are also
applied to determine the role of specific domains on the function of
these receptors. We are also investigating the molecular mechanisms
underlying the chemokines-regulated the inflammation-neurogenesis
coupling.
Selected Publications
Prado, G.N., Suetomi, K., Shumate, D., Maxwell, C., Ravindran, A., Rajarathnam, K., and Navarro J.
Chemokine Signaling Specificity: Essential Role for the
N-Terminal Domain of Chemokine Receptors. Biochemistry
46:8961-8968, 2007
Fuentes, L.Q., Reyes, C.E., Sarmiento, J.M., Villanueva, C.I., Figueroa, C.D., Javier Navarro, J.,
Gonzalez, C.B. Vasopressin up-regulates the expression of
growth-related immediate-early genes via two distinct EGF receptor
transactivation pathways. Cellular Signaling 20(9):1642-50, 2008
Sarmiento, J., Kypreos, K.E., Prado,
G.N., Suetomi, K., Stanzel, C., Maxwell, C., Shumate, D.,
Tandang-Silvas, M.R., Rajarathnam, K. and Navarro J.
Adenovirus mediated expression "in vivo" of
the chemokine receptor CXCR1. J. Struct. Funct. Genomics 10(1):17-23,
2009
Joseph, P.R., Sarmiento, J.M., Mishra, A.K., Das, S.T., Garofalo, R.P., Navarro J. and Rajarathnam, K. Probing the role of CXC motif in chemokine CXCL8 for high affinity binding and activation of CXCR1. J. Biol. Chem. 17;285(38):29262-9, 2010.
Sarmiento, J., Shumate, C., Suetomi, K., Ravindran, A., Villegas, L., Rajarathnam, K., Navarro J. Diverging mechanisms of activation of chemokine receptors revealed by novel chemokine agonists. PLoS One 6(12):e27967, 2011.
Ravindran, A., Sawant, K.V., Sarmiento, J., Navarro J and Rajarathnam K.
Chemokine CXCL1 dimer is a potent agonist for the CXCR2 receptor. J. Biol. Chem. 288(17):12244-52, 2013.
Link to PubMed Publications