
Miho Iijima, MS, PhD
Highlights
Languages
- English
Gender
FemaleJohns Hopkins Affiliations:
- Johns Hopkins School of Medicine Faculty
About Miho Iijima
Primary Academic Title
Professor of Cell Biology
Background
Dr. Miho Iijima is a professor of cell biology at the Johns Hopkins University School of Medicine. Her research focuses on lipid signaling in chemotaxis.
Dr. Iijima received her undergraduate degree in biology from the University of Tsukuba, Japan. She also earned her M.S. and Ph.D. in molecular biology from the University of Tsukuba. Dr. Iijima completed her postdoc in cell biology at Johns Hopkins University in 2004 and joined the Johns Hopkins faculty in 2006.
Dr. Iijima and her team are currently working to make a further connection between cells’ signaling events and directional movement. To this end, they have identified 17 new PH domain-containing proteins in addition to 10 previously known genes in the Dictyostelium cDNA and genome database. They also identified A PTEN homologue in Dictyostelium that is highly conserved with the human gene. They are disrupting all of these genes and studying their roles in chemotaxis.
Dr. Iijima has received a Beginning Grant-in-Aid from the American Heart Association from 2007 - 2009, earned a special fellowship from the Leukemia and Lymphoma Society, and was awarded The Albert L. Lehninger Award for Young Investigators from Johns Hopkins University School of Medicine in 2003.
Centers and Institutes
Research Interests
Lipid signaling chemotaxis
Lab Website
Iijima & Sesaki - Lab Website
Research Summary
Mechanisms of gradient sensing and chemotaxis are conserved in mammalian leukocytes and Dictyostelium amoebae. Both cells use G protein linked signaling pathways. PH domains specific for PtdIns(3,4)P2 and PtdIns(3,4,5)P3 bind to the membrane at the leading edge of the chemotaxing cell. This suggests that the local production of these phosphoinositides are regulated by PI3Ks and PTEN phosphatases and are a key component of directional sensing. The translocation of specific PH domain containing proteins at the leading edge likely regulates actin polymerization and pseudopud formation. Phosphoinositide secondary messengers may include members of the small GTPase Rho family, which have dramatic effects on the organization of the actin cytoskeleton. These GTPases are activated by guanine nucleotide exchange factors (GEFs). The GEFs for Rho/Rac/cdc42 each contain a PH domain and a catalytic Dbl homology domain, some of which have been shown to bind to the PIP3.
In order to make a further connection between signaling events and directional movement, Dr. Iijima and her team have identified 17 new PH domain-containing proteins in addition to 10 previously known genes in the Dictyostelium cDNA and genome database. Five of these genes contain both the Dbl and the PH domains, suggesting these proteins are involved in actin polymerization. A PTEN homologue has been also identified in Dictyostelium that is highly conserved with the human gene. They are disrupting all of these genes and studying their roles in chemotaxis.
Selected Publications
Igarashi, A., Itoh, K., Yamada, T., Adachi, Y., kato, T., Murata, D., Sesaki, H., and Iijima, M. (2018). Nuclear PTEN deficiency causes microcephaly with decreased neuronal soma size and increased seizure susceptibility. J. Biol. Chem. 5;293: 9292-9300
Nguyen, H-N., Yang, J.M., Afkari, Y., Park, B.H., Sesaki, H., Devreotes, P.N. and Iijima, M. (2014). Engineering ePTEN: an enhanced PTEN with increased tumor suppressor activities. Proc. Natl. Acad. Sci. USA. 111: E2684-2693
Senoo H, Kamimura K, Kimura R, Nakajima A, Sawai S, Sesaki H, Iijima M. (2019). Phosphorylated Rho-GDP directly activates mTORC2 Kinase toward AKT through dimerization with Ras-GTP to regulate cell migration. Nat. Cell Biol. 21: 867-878
Wang, Y., Senoo, H., Sesaki, H. and Iijima, M. (2013). Rho GTPases orient gradient sensing in chemotaxis. Proc. Natl. Acad. Sci. USA. 110: E4723-32
Yang, J.M., Schiapparelli, P., Nguyen, H-N., Igarashi, A., Zhang, Q., Abbadi, S., Amzel, L.M., Sesaki, H., Quiñones-Hinojosa, A., and Iijima, M. (2017). Characterization of PTEN mutations in brain cancer reveals that PTEN mono-ubiquitination promotes protein stability and nuclear localization. Oncogene. 36: 3673-3685
Honors
- Beginning Grant-in-Aid, American Heart Association, 1/1/07
- Special fellowship, Leukemia and Lymphoma Society, 1/1/04
- The Albert L. Lehninger Award for Young Investigators Johns Hopkins University School of Medicine, 1/1/03
- Special Fellowship, Japan Society for the Promotion of Science, 1/1/99
Graduate Program Affiliations
Biochemistry, Cellular and Molecular Biology Graduate Program
Additional Training
Johns Hopkins University, Baltimore, MD, 2004, Cell Biology