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My laboratory is interested in the structural and molecular basis for the signaling changes that allow tumors to spread by metastasis. Prevention of the spread of cancer cells from the primary tumor site is an important therapeutic approach for cancer treatment. Reduction of cell adhesion and enhancement of cell migration are key characteristics of cancer cells that are predisposed to metastasis. Recently, the MRL group of signaling adaptor proteins was found to be capable of regulating cell migration and adhesion by recruiting actin-binding proteins that mediate actin dynamics. Our research studies the recruitment of the MRL proteins to actin-binding proteins, and how this interaction regulates the cell adhesion and cell migration.  For this, we employ a combination of techniques, including X-ray crystallography, enzyme kinetics, mammalian cell culture, and genetic analysis. This research will contribute significantly to our understanding of the formation and regulation of cell adhesion and cell migration processes, and will facilitate the discovery of novel molecular targets for therapeutic intervention in cancer and other related diseases.

1. Wynne JP*, Wu J*, Su W, Mor A, Patsoukis N, Boussiotis VA, Hubbard SR, Philips MR. Rap1-interacting adapter molecule (RIAM) associates with the plasma membrane via a proximity detector. J Cell Biol. 2012 Oct 08. [Epub ahead of print]. *Equal contribution.
2. Ungureanu D, Wu J, Pekkala T, Niranjan Y, Young C, Jensen ON, Xu CF, Neubert TA, Skoda RC, Hubbard SR, Silvennoinen O. The pseudokinase domain of JAK2 is a dual-specificity protein kinase that negatively regulates cytokine signaling. Nat Struct Mol Biol. 2011 Aug 14. [Epub ahead of print] PubMed
3. Depetris RS*, Wu J*, Hubbard, S.R. Structural and functional studies of the Ras-associating and pleckstrin-homology domains of Grb10 and Grb14. Nat Struct Mol Biol. 2009;16,833-9. *Equal contribution. PubMed
4. Wu J*, Li W*, Craddock BP, Foreman KW, Mulvihill MJ, Ji QS, Miller WT, Hubbard SR. Small-molecule inhibition and activation-loop trans-phosphorylation of the IGF1 receptor. EMBO J. 2008;27,1985-94. *Equal contribution. PubMed
5. Wu J, Tseng Y, Xu C, Neubert TA, White MF, and Hubbard SR. Structural and biochemical characterization of the KRLB region in insulin receptor substrate-2. Nat Struct Mol Biol. 2008;15,251-8. PubMed
6. Bergamin E, Wu J, and Hubbard SR. Structural basis for phosphotyrosine recognition by suppressor of cytokine signaling-3. Structure. 2006;14,1285-92. PubMed
7. Wu J, Bera AK, Kuhn RJ, and Smith JL. Structure of the flavivirus helicase: implications for catalytic activity, protein interactions, and proteolytic processing. J Virol. 2005;79,10268-77. PubMed