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Research Interests:
Cell-extracellular matrix adhesion is a fundamental process that regulates cell shape, proliferation and differentiation. Abnormalities in cell-matrix adhesion and extracellular matrix assembly are closely associated with the pathogenesis of a variety of human diseases including cancer and diabetic nephropathy. The research in our laboratory focuses on the molecular mechanism by which cells regulate cell-matrix adhesion and signal transduction. Students and post-doctoral researchers who enter our laboratory will learn a wide variety of molecular and cell biological techniques including molecular cloning, mutagenesis, gene transfer, protein expression, yeast two-hybrid and other protein-protein interaction assays, hybridoma production, cell culture, cell adhesion, cell migration, immunofluorescence microscopy, immunoprecipitation, Northern, Southern and Western blotting, cell proliferation, apoptosis, and immunohistochemistry, and will have opportunities of developing new research projects and contributing to the advance of this exciting area in molecular and cellular pathology.
Selected Publications:
Tu, Y., Wu, S., Shi, X., Chen, K. and Wu, C. Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation. Cell (2003) 113(1): 37-47.
Fukuda, T., Guo, L., Shi, X. and Wu, C. CH-ILKBP regulates cell survival by facilitating the membrane translocation of Protein kinase B/Akt. J. Cell Biol. (2003) 160(7):1001-1008.
Velyvis, A., Vaynberg, J., Yang, Y., Vinogradova, O., Zhang, Y., Wu, C. and Qin, J. Structural and functional insights into PINCH LIM4 domain-mediated integrin signaling. Nature Structural Biology (2003) 10(7): 558-564
Li, J., Rao, H., Burkin, D., Kaufman, S.J. and Wu, C. The Muscle Integrin Binding Protein (MIBP) interacts with 7 1 integrin and regulates cell adhesion and laminin matrix deposition. Dev. Biol. (2003) 261(1): 209-219
Li, Y., Yang, J., Dai, C., Wu, C. and Liu, Y. Role for integrin-linked kinase in mediating tubular epithelial to mesenchymal transition and renal interstitial fibrogenesis. J. Clin. Invest. (2003) 112(4): 503-516
Attwell, S., Troussard, A., Mills, J., Wu, C. and Dedhar, S. Integration of 1 integrin-mediated cell attachment, cytoskeletal localization and signaling by Integrin-Linked Kinase (ILK), CH-ILKBP, and the tumor suppressor PTEN. Mol. Biol. Cell (2003) 14(12): 4813-4825
Fukuda, T., Chen, K., Shi, X. and Wu, C. PINCH-1 is an obligate partner of ILK functioning in cell shape modulation, motility and survival. J. Biol. Chem. (2003) 278(51): 51324-51333
Wu, C. The PINCH-ILK-parvin complexes: assembly, functions and regulation. Biochim. Biophys. Acta (2004) 1692(2-3):55-62
Zhang, Y., Chen, K., Tu, Y., and Wu, C. Distinct roles of two structurally closely related focal adhesion proteins, - and -parvins, in regulation of cell morphology and survival. J. Biol. Chem. (2004) 279(40):41695-41705
Wu, C. Migfilin and its binding partners: from cell biology to human diseases. J. Cell Sci. (2005) 118: 659-664
Gkretsi, V., Zhang, Y., Tu, Y., Chen, K., Stolz, D.B., Yang, Y., Watkins, S.C. and Wu, C. Physical and functional association of migfilin with cell-cell adhesions. J. Cell Sci. (2005) 118: 697-710
Vaynberg, J., Fukuda, T., Chen, K., Vinogradova, O., Velyvis, A., Tu, Y., Ng, L., Wu, C. and Qin, J. Structure of an ultraweak protein-protein complex and its crucial role in regulation of cell morphology and motility. Mol. Cell (2005) 17: 513-523
Qian, Y., Zhong, X., Flynn. D.C., Zheng, J.Z., Qiao, M., Wu, C., Dedhar, S., Shi, X., Jiang, B. H. ILK mediates actin filament rearrangements and cell migration and invasion through PI3K/Akt/Rac1 signaling. Oncogene (2005) 24(19): 3154-3165
Yang, Y., Guo, L., Blattner, S. M., Mundel, P., Kretzler, M. and Wu, C. The formation and phosphorylation of the PINCH-1-ILK- -parvin complex are important for regulation of renal glomerular podocyte adhesion, architecture and survival. J. Am. Soc. Nephrol. (2005) 16(7):1966-76
Sepulveda, J. L., Gkretsi, V. and Wu, C. Assembly and signaling of adhesion complexes. Curr. Top. Dev. Biol. (2005) 68: 183-225
Xu, Z., Fukuda, T., Li, Y., Zha, X., Qin, J. and Wu, C. Molecular dissection of PINCH-1 reveals a mechanism of coupling and uncoupling of cell shape modulation and survival. J. Biol. Chem. (2005) 280(30): 27631-27637
Wu, C. PINCH, N(i)ck and the ILK: network wiring at cell-matrix adhesions. Trends in Cell Biology (2005) 15(9):460-466
Chen, H., Huang, X. N., Chen, K., Guo, L., Tummalapali, L., Dedhar, S., St.-Arnaud, R., Wu, C., and Sepulveda, J. L. Role of the integrin-linked kinase/PINCH1/alpha-parvin complex in cardiac myocyte hypertrophy. Lab. Invest. (2005) 85(11):1342-56
Yaroslavskiy, B. B., Zhang, y., Kalla, S. E., Palacios, V. G., Li, Y., Zaidi, M., Wu, C. and Blair, H. C. NO-dependent Osteoclast Motility: Cytoskeletal Rearrangement by cGMP-dependent Protein Kinase I via VASP and Calcium-dependent Mechanisms. J. Cell Sci. (2005): 118(23):5479-87
Sepulveda, J. L. and Wu, C. The Parvins. Cell. Mol. Life Sci. (2006): 63(1):25-35
Zhang, Y., Tu, Y., Gkretsi, V. and Wu, C. Migfilin interacts with VASP and regulates VASP localization to cell-matrix adhesions and migration. J. Biol. Chem. (2006): 281(18):12397-407
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