Researcher Profile

Estela Jacinto, PhD

Associate Professor of Biochemistry and Molecular Biology
Robert Wood Johnson Medical School
Rutgers, The State University of New Jersey

RWJMS Research and School of Public Health Bldg.
683 Hoes Lane West, 2nd Floor
Piscataway, NJ 08854

Phone: (732) 235-4476
Email: jacintes@rwjms.rutgers.edu

Assistant: Letice Smith
(732) 235-4551
Email: smithla@rwjms.rutgers.edu


Research Program Alignment

Membership Type: Full


Research Interests

  • Cancer
  • Protein Kinases/mTOR/Akt Signaling
  • Lymphoma
  • T Cell
  • Protein Folding
  • Insulin
  • Translation

Selected Publications

Kim, S.J., DeStefano, M., Oh, W.J., Wu, C., Vega-Cotto, N.M., Finlan, M., Liu, D., Su, B., and Jacinto, E. mTOR complex 2 regulates proper turnover of insulin receptor substrate-1 via the ubiquitin ligase Fbw8. Molecular Cell 2012, in press.

Oh, W., Wu, C., Kim, S.J., Facchinetti, V., Julien, L.A., Finlan, M., Roux, P.P., Su, B., and Jacinto, E. mTORC2 associates with ribosomes to promote cotranslational phosphorylation and stability of nascent Akt polypeptide. EMBO J. 2010; 29, 3939-3951.
Nominated 2010 Signaling Breakthroughs of the Year, Science Signal. 4 (154): 1-7.
Editors' Choice Highlight: Science Signal. 3, ec369, 2010; Cell 144: 460.

Facchinetti, V., Ouyang, W., Wei, H., Soto, N., Lazorchak, A., Gould, C., Lowry, C., Newton, A.C., Mao, Y., Miao, R.Q., Sessa, W.C., Qin, J., Zhang, P., Su, B., and Jacinto, E. The mammalian target of rapamycin complex 2 controls folding and stability of Akt and protein kinase C. EMBO J 2008; 27, 1932-1943.

Jacinto, E. *, Facchinetti*, V., Liu, D., Soto, N., Wei, S., Jung, S.Y., Huang, Q., Qin, J., and Su, B. SIN1/MIP1 maintains rictor-mTOR complex integrity and regulates Akt phosphorylation and substrate specificity. Cell 2006; 127, 125-137. *equal contribution
(Highlighted in Dev. Cell 11:433)

Jacinto, E.*, Loewith, R.*, Schmidt, A., Lin, S., Ruegg, M., Hall, A., and Hall, M.N. Mammalian TOR complex 2 (mTORC2) controls the actin cytoskeleton and is rapamycin insensitive. Nature Cell Biology 2004; 6, 1122-1128. *equal contribution

Bonenfant, D., Schmelzle, T., Jacinto, E., Crespo, J.L., Mini, T., Hall, M.N., and Jenoe, P. Quantitation of changes in site specific phosphorylation: a simple method based on stable isotope labelling and mass spectrometry. Proc. Natl. Acad. Sci. 2003; 100, 880-885.

Loewith, R., Jacinto, E., Wullschleger, S., Lorberg, A., Crespo, J.L., Bonenfant, D., Oppliger, W., Jenoe, P., and Hall, M.N. Two TOR complexes, only one of which is rapamycin sensitive, have distinct roles in cell growth control. Molecular Cell 2002; 10, 457-468.

Jacinto, E., Guo, B., Arndt, K.T., Schmelzle, T., and Hall, M.N. TIP41 interacts with TAP42 and negatively regulates the TOR signaling pathway. Molecular Cell 2001;8, 1017-1026.

Werlen, G., Jacinto, E., Xia, Y., and Karin, M. Calcineurin preferentially synergizes with PKC-theta to activate JNK in T lymphocytes. EMBO J 1998; 17, 3101-3111.

Jacinto, E., Werlen, G., and Karin, M. Cooperation between Syk and Rac1 leads to synergistic JNK activation in T lymphocytes. Immunity 1998;8, 31-41.

Wu, Z., Wu, J., Jacinto, E., and Karin, M. Molecular cloning and characterization of human JNKK2, a novel Jun N-terminal kinase (JNK)-specific kinase. Mol. Cell. Biol 1997;17, 7407-7416.

Su, B., Jacinto, E., Hibi, M., Kallunki, T., Karin, M., and Ben-Neriah, Y. JNK is involved in signal integration during costimulation of T lymphocytes. Cell 1994; 77, 727-736.

The content for this Research Profile is maintained by Paul Novembre (novembre@cinj.rutgers.edu)