Dr. Kurokawa, a native of Japan, received a Bachelor of Veterinary Medicine (equivalent to the D.V.M. in the United States) from Hokkaido University. He moved to the United States to pursue doctoral work at the University of Massachusetts Amherst, studying the signaling mechanisms of fertilization under the supervision of Dr. Rafael Fissore. Dr. Kurokawa conducted his postdoctoral research in the laboratory of Dr. Sally Kornbluth at Duke University Medical Schol, studying the regulation of apoptosis in cancer. Before joining Kent State University, he spent five years in the Department of Pharmacology & Toxicology (subsequently Molecular & Systems Biology) at the Geisel School of Medicine at Dartmouth College as an Assistant Professor.
The broad goal of Dr. Kurokawa’s research program is to investigate the molecular mechanisms of cancer development and drug resistance. In particular, his research centers on two areas of investigation: 1) the role of the ubiquitin E3 ligase HUWE1 in the p53 tumor suppressor pathway, and 2) the regulation of lipid metabolism in tumor development and drug resistance. His laboratory utilizes novel mouse models together with modern molecular and biochemical techniques to address these questions. Dr. Kurokawa has published over 40 peer-reviewed articles and book chapters (the most updated listing of papers from the Kurokawa Lab can be found in Google Scholar; https://scholar.google.com/citations?user=mkso-TAAAAAJ&hl=en). His work has been supported in part by the National Cancer Institute, the American Cancer Society, the Mary Kay Foundation, and the Cancer Research Institute.
B.Vet.Med., Hokkaido University, Sapporo, Japan, Ph.D., University of Massachusetts Amherst, Postdoc, Duke University
Kurokawa, M., Zhao, C., Reya, T., Kornbluth, S. 2008. Inhibition of apoptosome formation by suppression of Hsp90β phosphorylation in tyrosine kinase-induced leukemias. Molecular and Cellular Biology 28, 5494-5506.
Nutt, L.K., Buchakjian, M.R., Gan, E., et al., 2009. Metabolic control of oocyte apoptosis mediated by 14-3-3-regulated dephosphorylation of caspase-2. Developmental Cell 16, 856-866.
Kurokawa, M., Kornbluth, S. 2009. Caspases and kinases in a death grip. Cell 138, 838-854.
Kurokawa, M., Kornbluth, S. 2010. Stalling in mitosis and releasing the apoptotic brake. EMBO Journal 29, 2255-2257.
Kim, J., Parrish, A.B., Kurokawa, M., Matsuura, K., Freel, C.D., Andersen, J.L., Johnson, C.E., Kornbluth, S. 2012. Rsk-mediated phosphorylation and 14-3-3ε binding of Apaf-1 suppresses cytochrome c-induced apoptosis. EMBO Journal 13, 1279-1292.
Kurokawa, M., Ito, T., Yang, C.S., et al., 2013. Engineering a BCR-ABL-activated caspase for the selective elimination of leukemic cells. Proceedings of the National Academy of Sciences 110, 2300-2305.
Kurokawa, M., Kim, J., Geradts, J., et al., 2013. A network of substrates of the E3 ligases MDM2 and HUWE1 control apoptosis independently of p53. Science Signaling 6, Ra32.
McCoy, F., Darbandi, R., Lee, H.C., et al., 2013. Metabolic activation of CaMKII by Coenzyme A. Molecular Cell 52, 325-339.
Fernald, K., Kurokawa, M. 2013. Evading apoptosis in cancer. Trends in Cell Biology 23, 620-633.
Henao, R., Geradts, J., Kurokawa, M., Kornbluth, S., Lucas, J.E. 2014. Automated, quantitative analysis of histopathological staining in nuclei. AMIA Joint Summits on Translational Science Proceeding 2014, 54–59.
Canfield, K., Li, J., Wilkins, O.M., et al., 2015. ERBB4 tyrosine kinase mediates acquired resistance to ERBB2 inhibitors in breast cancer cells. Cell Cycle 14, 648-655.
Li, J., Kurokawa, M. 2015. Regulation of MDM2 stability after DNA damage. Journal of Cellular Physiology 230, 2318–2327.
Canfield, K., Wells, W., Geradts, J., et al., 2016. Inverse association between MDM2 and HUWE1 protein expression levels in human breast cancer and liposarcoma. International Journal of Clinical and Experimental Pathology 9, 6342-6349.
Matsuura, K., Canfield, K., Feng W., Kurokawa, M. 2016. Metabolic regulation of apoptosis in cancer. International Review of Cell & Molecular Biology 327, 43-87.
Deming P.B. Kurokawa, M., 2017. Dismantling the Apoptotic Cell by Caspases. eLS. 1–10.
Bang, S., Bhatt H.C., Chen Y.Y., Kurokawa, M. 2018. MDM2 In: Choi, S (ed). Encyclopedia of Signaling Molecules, Second Edition, Volume 5, 3021-3028. Springer. [Book Chapter]
Huang A., Yang, E., Kurokawa, M. 2018. MDM4 In: Choi, S (ed). Encyclopedia of Signaling Molecules, Second Edition, Volume 5, 3028-3034. Springer. [Book Chapter]
Feng, W.W., Wilkins, O.M., Bang, S., Ung, M., Li, J. , An, J., del Genio, C.L., Canfield, K., DiRenzo, J., Wells, W., Gaur, A., Robey, R.B., Guo J.Y., Powles, R.L., Sotiriou, C., Pusztal L., Febbraio, M., Cheng, C., Kinlaw, W.B., Kurokawa, M. 2019. CD36-m
Bang, S., Kaur, S., Kurokawa, M. 2020. Regulation of the p53 family proteins by the ubiquitin proteasomal pathway. International Journal of Molecular Sciences 21, 216.
Feng, W.W., Bang, S., Kurokawa, M. 2020. CD36: a key mediator of resistance to HER2 inhibitors in breast cancer. Molecular & Cellular Oncology 7(2), 1715766.
Cassidy, K.B.*, Bang, S.*, Kurokawa, M.**, Gerber, S.A.** Direct regulation of Chk1 protein stability by E3 ubiquitin ligase HUWE1. The FEBS Journal (* co-first authors, ** co-corresponding authors) In Press
Feng, W.W., Kurokawa, M. Lipid metabolic reprogramming as an emerging mechanism of resistance to kinase inhibitors in breast cancer. Cancer Drug Resistance In Press