Welcome to Uruno Lab
Kyushu University
Advanced Research Initiative, Medical Institute of Bioregulation
~~~~~~Join Us~~~~~~
We welcome highly motivated postdoctoral researchers and graduate students who are interested in pursuing long-term research training in our laboratory.
Our team is dedicated to research excellence while valuing a healthy work-life balance. We actively support the career development of our members and are committed to helping them grow as independent researchers.
Kyushu University offers a wide range of outstanding programs and resources to support early-career scientists. Individuals seeking full-time research positions in a stimulating and collaborative environment are encouraged to contact us.
@Takehito
2025 June
Education
・The University of Tokyo, Faculty of Pharmaceutical Sciences (1985-1989)
・The University of Tokyo, Graduate School of Pharmaceutical Sciences (1989-1994)
Ph.D. (Pharmaceutical Sciences)
Employment
・National Institute of Bioscience and Human-Technology, Agency of Industrial Science and Technology, Tsukuba, Japan (1994-1999)
・The Jerome H. Holland Laboratory for Biomedical Sciences, American Red Cross, Maryland, USA (1999-2004)
・Northwestern University Medical School, Visiting scientist, Chicago, USA (2001.2)
・National Heart, Lung, and Blood Institute, National Institutes of Health (NIH), Maryland, USA (2004-2008) ; Senior Research Fellow, Staff (2006-2008)
・RIKEN Center for Developmental Biology, Kobe, Japan (2008-2009)
・Kyushu University, Medical Institute of Bioregulation, Fukuoka, Japan (2009-current): Associate Professor since 2.1.2014.
Physiological homeostasis in the body is maintained through complex interactions and signal transduction among diverse cell types. Disruption of these processes contributes to the development of various diseases and aging. Our research aims to elucidate the molecular mechanisms underlying cancer, immune disorders, and allergic diseases by focusing on signal transduction pathways that regulate cytoskeletal dynamics and metabolic processes. We further seek to translate these findings into drug discovery and therapeutic strategies.
Currently, we investigate the pathophysiological roles of enzymatic sulfation and its metabolites in cancer–immune interactions within the tumor microenvironment, as well as in host–pathogen interactions during infectious diseases. In addition, we are exploring how acoustic stimuli influence metabolism and physiological responses in mammals with the long-term goal of societal and biomedical applications.
"Through original research, we aim to deepen our understanding of biology and contribute to human health."
Takehito URUNO, Ph.D.
Associate Professor
Advanced Research Initiative
Medical Institute of Bioregulation, Kyushu University
tel: +81-092-642-6797/6830
e-mail: uruno.takehito.694 (((at))) m.kyushu-u.ac.jp
e-mail: uruno (((at))) bioreg.kyushu-u.ac.jp
PUBLICATIONS:
1. Aihara R, Takahashi M et al.
Phospholipase D1 is a critical mediator of neutrophil extracellular trap formation and venous thrombosis.
Front Immunol 16: 1666184 (2025)
2. Tatsuguchi T, Uruno T et al.
Cancer-derived cholesterol sulfate is a key mediator to prevent tumor infiltration by effector T cells.
Int Immunol 34: 277-89 (2022)
3. Kamikaseda Y, Uruno T, et al.
Targeted inhibition of EPAS1-driven IL-31 production by a small-molecule compound.
J Allergy Clin Immunol 148(2):633-638 (2021)
4. Sakurai T, Kukimoto-Niino M et al.
A conserved PI(4,5)P2-binding domain is critical for immune regulatory function of DOCK8.
Life Sci Alliance 4: e202000873 (2021)
5. Sakurai T, Uruno T et al.
Cholesterol sulfate is a DOCK2 inhibitor that mediates tissue-specific immune evasion in the eye.
Sci Signal 11: eaao4874 (2018)
6. Tajiri H, Uruno T, et al.
Targeting Ras-Driven Cancer Cell Survival and Invasion through Selective Inhibition of DOCK1.
Cell Rep 9: 969-980 (2017)
7. Yamamura K, Uruno T, et al.
The transcription factor EPAS1 links DOCK8 deficiency to atopic skin inflammation via IL-31 induction.
Nat Commun 8:13946 (2017)
8. Zwolak A, Uruno T, et al.
Molecular basis for barbed end uncapping by CARMIL homology domain 3 of mouse CARMIL-1.
J Biol Chem 285:29014-26 (2010)
9. Uruno T, Remmert K, Hammer JA.
CARMIL is a potent capping protein antagonist: identification of a conserved CARMIL domain that inhibits the activity of capping protein and uncaps capped actin filaments.
J Biol Chem 281:10635-50 (2006)
10. Uruno T, Liu J, et al.
Sequential interaction of actin-related proteins 2 and 3 (Arp2/3) complex with neural Wiscott-Aldrich syndrome protein (N-WASP) and cortactin during branched actin filament network formation.
J Biol Chem 278:26086-93 (2003)
11. Uruno T, Liu J, et al.
Activation of Arp2/3 complex-mediated actin polymerization by cortactin.
Nat Cell Biol 3:259-66 (2001)