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Jess Cunnick, PhD

Assistant Professor of Cell Biology
Department of Basic Sciences
Geisinger Commonwealth Research Department
North Campus

Geisinger Commonwealth School of Medicine
Medical Sciences Building
525 Pine St.
Scranton, PA 18509
Fax: 570-504-9639

Research interests

Jess Cunnick, PhD, is assistant professor of cell biology in the Department of Basic Sciences. Dr. Cunnick received his PhD from Kansas State University and completed his postdoctoral work at the H. Lee Moffitt Cancer Center and Research Institute in Tampa, FL. His research interests are in actin cytoskeleton and associated proteins.

The actin cytoskeleton is vital for numerous cellular processes including cell division, cell adhesion, cell migration and the maintenance of cell shape. The organization of this dynamic network of actin filaments is regulated by numerous actin filament cross-linking proteins and cellular signaling pathways. Our research focuses on the function of a protein called actin filament-associated protein 1 or AFAP1 that is found in both actin stress fibers and podosomes. Stress fibers are long bundles of actin filaments and associated proteins that are involved in the regulation of cell contractility, migration and cell shape. Podosomes are dynamic, actin-rich punctate structures that function both to adhere to and degrade the extracellular matrix through the release of proteases. These structures are found in cells that can cross tissue barriers such as monocytic cells, vascular smooth muscle cells, endothelial cells and carcinoma cells. In cancer cells these structures are referred to as invadopodia. Therefore, podosomes and invadopodia are thought to facilitate the invasiveness of cells. Our laboratory is attempting to define the role of AFAP1 in regulating the dynamics of podosomes. This research may have implications for pathological conditions ranging from atherosclerosis to cancer.

Student research opportunities

The cellular actin cytoskeleton is vital for numerous cellular processes including migration, proliferation and differentiation. Dr. Cunnick’s lab studies how an actin filament‐associated protein, AFAP1, and interacting cell signaling proteins, contribute to the regulation of cellular processes that depend on the integrity of the actin cytoskeleton. One major group of AFAP1 interacting proteins is the Src kinase protein family. The prototypical member of this family is the proto‐oncogene c‐Src, whose activity is enhanced in a number of cancers. AFAP1, through its interaction with c‐Src and other proteins, has been shown to be involved in the formation of cellular protrusions that facilitate cancer cell invasion. However, Src family proteins have also been shown to regulate a large number of physiological processes, including glucose and lipid metabolism. Our lab has developed a mouse model that no longer expresses AFAP1, a knockout mouse. Using this mouse model our lab is investigating the mechanism by which AFAP1 and Src kinase protein partners regulate actin cytoskeleton dependent cellular processes and physiological processes such as glucose and lipid metabolism. The knowledge gained from our research will provide a better understanding of cancers where the disturbance of c‐Src‐mediated cellular processes might directly contribute to cancer progression and also signaling pathways that contribute to metabolic diseases, such as diabetes.

Recent publications

  • Cho, Y., Silverstein, R., Geisinger, M., Martinkovich, S., Cunnick, J., Planey, SL., Arnott, JA. AFAP1 is a novel downstream mediator of TGF-β1 for CCN2 induction in osteoblasts. PlosOne. 2015. [in press]
  • Cunnick JM, Kim S, Hadsell J, Collins S, Cerra C, Reiser P, Flynn D, Cho YJ. Actin filament-associated protein 1 is required for cSrc activity and secretory activation in the lactating mammary gland. Oncogene 0, (21 July 2014) | doi:10.1038/onc.2014.205
  • Snyder BN, Cho Y, Qian Y, Coad JE, Flynn DC, Cunnick JM. AFAP1L1 is a novel adaptor protein of the AFAP family that interacts with cortactin and localizes to invadosomes. Eur J Cell Biol. 2011 May;90(5):376-89. Full Text
  • Dorfleutner, A., Cho, YJ., Vincent, D., Cunnick, J., Lin, H., Weed, S., Stehlik, C., and Flynn, D.C. Phosphorylation of AFAP-110 affects podosome lifespan in A7r5 cells. Journal of Cell Science 121: 2394-2405, 2008. Full Text
  • Flynn, D.C., Cho, YJ., Vincent, D., and Cunnick, J.M. Podosomes and invadopodia: Related structures with common protein components that may promote breast cancer cellular invasion. Breast Cancer: Basic and clinical research 1: 1-13, 2008. Full Text
  • Cho, YJ.*, Cunnick, J.M.*, Yi, SJ., Kaartinen, V., Groffen, J. and Heisterkamp, N. Abr and Bcr, two homologous Rac GTPase-activating proteins, control multiple cellular functions of murine macrophages. Molecular and Cellular Biology. 27(3): 899-911, 2007. (*Co-first authors) Full Text
  • Cunnick, J., Kaur, P., Cho, Y., Groffen, J. and Heisterkamp, N. Use of bone marrow-derived macrophages to model murine innate immune responses. J Immunol Methods. 311(1-2): 96-105, 2006. Full Text
  • Mishra, S., Zhang, B., Cunnick, J.M., Heisterkamp, N. and Groffen, J. Resistance to Imatinib of bcr/abl p190 lymphoblastic leukemia cells. Cancer Res. 66(10): 5387-93, 2006. Full Text
  • Mishra, S., Reichert, A., Cunnick, J., Senadheera, D., Hemmeryckx, B., Heisterkamp, N., Groffen, J. Protein kinase CKII alpha interacts with the Bcr moiety of Bcr/Abl and mediates proliferation of Bcr/Abl-expressing cells. Oncogene 22: 8255-62, 2003. Full Text
  • Cunnick, J.M., Meng, S., Ren, Y., Desponts, C., Wang, H. G., Djeu, J. Y., Wu, J. Regulation of the mitogen-activated protein kinase signaling pathway by SHP2. J. Biol. Chem. 277: 9498-9504, 2002. Full Text
  • Dorsey, J. F., Cunnick, J.M., Lanehart, R., Huang, M., Kraker, A. J., Bhalla, K. N., Jove, R., and Wu, J. Interleukin-3 protects Bcr-Abl-transformed hematopoietic progenitor cells from apoptosis induced by Bcr-Abl tyrosine kinase inhibitors. Leukemia 16: 1589-1595, 2002. Full Text
  • Dorsey, J.F., Cunnick, J.M., and Wu, J. Regulation of the Erk2-Elk1 signaling pathway and megakaryocytic differentiation of Bcr-Abl+ K562 leukemic cells by Gab2. Blood 99: 1388-1397, 2002. Full Text
  • Wu, J. and Cunnick, J.M. Trans-regulation of epidermal growth factor receptor by lysophosphatidic acid and G protein-coupled receptors. Biochim. Biophys. Acta 1582: 100-106, 2002. Full Text
  • Kim SO, Loesch K, Wang X, Jiang J, Mei L, Cunnick JM, Wu J, Frank SJ. A role for Grb2-associated binder-1 in growth hormone signaling. Endocrinology 143: 4856-67, 2002. Full Text
  • Cunnick, J.M., Mei, L., Doupnik, C.A., and Wu, J. Phosphotyrosines 627 and 659 of Gab1 constitute a bisphosphoryl tyrosine-based activation motif (BTAM) conferring binding and activation of SHP2. J. Biol. Chem. 276: 24380-24387, 2001. Full Text
  • Cunnick, J.M., Dorsey, J., Munoz-Antonia, T., Mei, L., and Wu, J. Requirement of SHP2 binding to Grb2-associated binder-1 for mitogen-activated protein kinase activation in response to lysophosphatidic acid and epidermal growth factor. J. Biol. Chem. 275: 13842-13848, 2000. Full Text
  • Sekharam, M., Cunnick, J.M., and Wu, J. Involvement of lipoxygenase in lysophosphatidic acid-stimulated hydrogen peroxide release in human HaCaT keratinocytes. Biochem. J. 15: 751-758, 2000.
  • Cunnick, J.M., Dorsey, J.F., Mei, L., and Wu, J. Reversible regulation of SHP-1 tyrosine phosphatase activity by oxidation. Biochem. Mol. Biol. Int. 45: 887-94, 1998. Full Text
  • Cunnick, J.M., Dorsey, J.F., Standley, T., Turkson, J., Kraker, A.J., Fry, D.W., Jove, R., and Wu, J. Role of tyrosine kinase activity of epidermal growth factor receptor in the lysophosphatidic acid-stimulated mitogen-activated protein kinase pathway. J. Biol. Chem. 273: 14468-75, 1998. Full Text
  • Sekharam, M., Trotti, A., Cunnick, J.M., and Wu, J. Suppression of fibroblast cell cycle progression in G1 phase by N-acetylcysteine. Toxicol. Appl. Pharmacol. 149: 210-6, 1998. Full Text


Bachelor – McPherson College, McPherson, KS 
PhD – Kansas State University, Manhattan, KS 
Postdoctoral – Moffitt Cancer Center, Tampa, FL