Dr. Partha Roy is an Associate Professor of Bioengineering, Cell Biology, and Pathology at the University of Pittsburgh. He received his BS in Mechanical Engineering from Jadavpur University (India), MS in Biomedical Engineering from the Indian Institute of Technology, Madras (Thesis title: Finite element analyses of scoliosis), and PhD in Biomedical Engineering from the University of Texas Southwestern Medical Center, Dallas, Texas (Dissertation title: An in vitro force measurement system to study corneal cell-matrix interaction). After completing his post-doctoral fellowships in Cell Biology at Harvard Medical School and University of North Carolina, Chapel Hill (specializations: cell migration, photomanipulation of proteins), he began his independent academic career at the University of Pittsburgh.

Dr. Roy is a member of the American Society for Cell Biology, the American Association of Cancer Research, and the Biomedical Engineering Society. He is an associate editor of Cellular and Molecular Bioengineering. His laboratory currently has three major research areas (primarily in the field of cancer and angiogenesis) as summarized below:

• Directed cell migration plays an important role in embryonic development, wound healing, angiogenesis, immune response, cancer invasion, and metastasis. Dynamic reorganization of actin cytoskeleton, a key aspect of cell migration, is regulated by the concerted actions of various classes of actin-binding proteins (ABPs), and some of these ABPs are fundamental drivers of actin-based cell motility. Altered expressions and activities of fundamental drivers of cell migration are correlated with aberrant cell motility in pathologic scenarios. The main research efforts are to 1) gain novel insights on how dysregulation of fundamental drivers of cell migration contributes to metastatic progression of solid cancers, 2) study fundamental aspects of angiogenesis, and 3) develop translational strategies (through collaborative efforts centered on virtual screening of compound library and unbiased small molecule screening followed by functional assays) exploiting the pathways of dysregulation as means to suppress metastatic phenotype of cancer cells and angiogenesis-dependent pathology.
• Post-translational modification plays a crucial role in regulating protein activities. Novel post-translational modifications of ABPs and how they impact protein function and actin-dependent biological processes are studied.
• MKL/SRF-mediated gene transcription is a highly conserved mechanism that connects dynamic reorganization of actin cytoskeleton to gene expression control. Novel signaling pathways downstream of MKL are being explored in the context of regulation of actin-based biological processes.

Selected publications:

• Roy P., Rajfur Z., Jones D., Marriott G., Loew L., Jacobson K. (2001): Local photorelease of caged-Tb4 in locomoting keratocytes causes cell turning. Journal of Cell Biology 153 (5): 1035-1048.
• Roy P., Rajfur Z., Pomorski P., Jacobson K. (2002): Microscope-based techniques for studying cell adhesion and migration. Nature Cell Biology 4(4): E91-96.
• Rajfur Z., Roy P., Otey C., Romer L., Jacobson K. (2002): Dissecting the link between stress fibers and focal adhesions by CALI of EGFP-fusion proteins. Nature Cell Biology 4(4): 286-293.
• Ding Z., Lambrechts A., Parepally M., Roy P. (2006): Silencing profilin-1 inhibits endothelial cell proliferation, migration and cord morphogenesis. Journal of Cell Science 119: 4127-4137. PMID: 16968742
• Zou L., Jaramillo M., Whaley D., Wells A., Panchapakesa V., Das T., Roy P. (2007): Profilin-1 is a negative regulator of mammary carcinoma aggressiveness. British Journal of Cancer 97: 1361-1371. PMCID: PMC2360229
• Das T., Bae Y, Wells A., and Roy P. (2009): Profilin-1 overexpression upregulates PTEN and suppresses AKT activation in breast cancer cells. Journal of Cell Physiology 218(2): 436-443. PMCID: PMC2874249
• Bae Y., Ding Z., Zou L., Wells A., Gertler F., Roy P. (2009): Loss of Profilin-1 expression enhances breast cancer cell motility by Ena/VASP proteins Journal of Cell Physiology 219(2):354-364. PMCID: PMC2990882
• Leloup L., Hanshuang S., Bae , Deasy B., Stolz D., Roy P., Wells A (2010)  m-Calpain activation is regulated by its membrane localization and by its binding to phosphatidylinositol 4,5-bisphosphate. J. Biol Chem 285(43):33549-66 PMCID: PMC2963356
• Bae Y., Ding Z., Das T. Wells A., Gertler F., Roy P. (2010): Profilin1 regulates PI(3,4)P₂ and lamellipodin accumulation at the leading edge thus influencing motility of MDA-MB-231 cells PNAS 107(50): 21547-21552 PMID: 21115820.
• Ding Z., Roy P. (2013) Profilin-1 vs -2: Two faces of the same coin? Breast Cancer Research 27; 15(3):311. PMID: 23827010
• Ding Z., Joy M.^., Bhargava R., Gunsaulus M., Lakshman N^., Miron-Mendoza M.^, Petroll M., Condeelis J., Wells A., Roy P. (2014) Profilin-1 downregulation has contrasting effects on early vs late steps of breast cancer metastasis Oncogene 33(16):2065-74. PMID: 23686314
• Joy M., Vollmer L., Hulkower K., Peterson C., Dutch Boltz R., Stern A., Roy P*., Vogt V. (2014) A high-content, multiplexed screen in human breast cancer cells identifies profilin-1 inducers with anti-migratory activities PLOS ONE Feb 10;9(2):e88350. doi: 10.1371/journal.pone. 0088350. [* – co-corresponding author] PMID: 24520372.
• Gau D., Lesnock J., Hood B., Bhargava R., Sun M., Darcy K., Conrads T., Edwards R., Kelley J., Krivak T., Roy P. (2015) BRCA1 deficiency in ovarian cancer is associated with alteration in expression of several key regulators of cell motility – A proteomics study. Cell Cycle 14(12):1884-92. PMID: 25927284.
• Jiang C., Veon W., Li H, Hallows K., Roy P. (2015) Epithelial morphological reversion drives Profilin-1-induced elevation of p27^kip1 in mesenchymal triple-negative human breast cancer cells through AMPK activation Cell Cycle Jul 15:1-10.

Gau D., Veon W., Zeng X., Yates N., Shroff S., Koes D., Roy P (2016) Threonine 89 is an important residue of profilin-1 that is phosphorylatable by protein-kinase A, PLOS one 11(5):e0156313. doi: 10.1371/journal.pone.0156313.