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chun-chun LiAssociate Professor
E - Mail
Office Phone
+886-6-275-7575 ext.58135
Laboratory Phone
58104 or 58114轉34
Highest Education
Brief Biography
2013/08–Present Assistant Professor, Department of Life Sciences, National Cheng Kung University
2008/10–2013/07 Postdoctoral Research Fellow, National Institutes of Health (NIH), USA
2007/09–2008/09 Postdoctoral Research Fellow, Institute of Molecular Medicine, National Taiwan University
2008/10–2013/07 Postdoctoral Research Fellow, National Institutes of Health (NIH), USA
2007/09–2008/09 Postdoctoral Research Fellow, Institute of Molecular Medicine, National Taiwan University
Research Areas
Research Directions:
Cell migration plays an important role in embryonic development, immune surveillance, and wound healing. Directed cell migration is typically induced by extracellular chemical or mechanical signals and requires precise spatial and temporal coordination between vesicular trafficking and cytoskeletal reorganization. Many molecules are known to regulate the generation and maintenance of directed cell migration. Although individual molecular mechanisms have been elucidated, how vesicular trafficking and cytoskeletal remodeling are coordinated remains unclear. Small GTPases of the ADP-ribosylation factor (Arf) family and their regulators, guanine nucleotide-exchange factors (GEFs), may serve as key links between these processes.
The Arf GEFs BIG1 and BIG2 activate Arf by promoting GTP binding via their Sec7 domain, thereby participating in vesicular trafficking or activating enzymes that modify phospholipids. In addition to the central Sec7 domain, BIG1 and BIG2 contain several N- and C-terminal domains whose functions remain unclear. Mutations in the BIG2 gene have been identified in human autosomal recessive periventricular heterotopia and microcephaly. Our previous studies showed that BIG1 and BIG2 regulate actin cytoskeleton dynamics and thereby affect cell migration. siRNA-mediated knockdown of BIG1 or BIG2 increases F-actin levels and reduces membrane protrusion, leading to impaired cell motility.
However, the upstream regulatory molecules and signaling pathways of BIG1 and BIG2, as well as the molecular mechanisms by which they regulate cell migration, remain unclear. We aim to use a combination of cell biology, molecular biology, biochemistry, and proteomics approaches to identify and investigate the functions of BIG1/2 protein complexes in vesicular trafficking and cell migration, as well as the role of Arf in these processes. The goal is to elucidate the molecular regulatory mechanisms by which BIG1 and BIG2 participate in vesicular transport and cell migration. The results will improve our understanding of diseases caused by dysfunction in small GTPases and their regulators, and may provide insights for therapeutic strategies.
Cell migration plays an important role in embryonic development, immune surveillance, and wound healing. Directed cell migration is typically induced by extracellular chemical or mechanical signals and requires precise spatial and temporal coordination between vesicular trafficking and cytoskeletal reorganization. Many molecules are known to regulate the generation and maintenance of directed cell migration. Although individual molecular mechanisms have been elucidated, how vesicular trafficking and cytoskeletal remodeling are coordinated remains unclear. Small GTPases of the ADP-ribosylation factor (Arf) family and their regulators, guanine nucleotide-exchange factors (GEFs), may serve as key links between these processes.
The Arf GEFs BIG1 and BIG2 activate Arf by promoting GTP binding via their Sec7 domain, thereby participating in vesicular trafficking or activating enzymes that modify phospholipids. In addition to the central Sec7 domain, BIG1 and BIG2 contain several N- and C-terminal domains whose functions remain unclear. Mutations in the BIG2 gene have been identified in human autosomal recessive periventricular heterotopia and microcephaly. Our previous studies showed that BIG1 and BIG2 regulate actin cytoskeleton dynamics and thereby affect cell migration. siRNA-mediated knockdown of BIG1 or BIG2 increases F-actin levels and reduces membrane protrusion, leading to impaired cell motility.
However, the upstream regulatory molecules and signaling pathways of BIG1 and BIG2, as well as the molecular mechanisms by which they regulate cell migration, remain unclear. We aim to use a combination of cell biology, molecular biology, biochemistry, and proteomics approaches to identify and investigate the functions of BIG1/2 protein complexes in vesicular trafficking and cell migration, as well as the role of Arf in these processes. The goal is to elucidate the molecular regulatory mechanisms by which BIG1 and BIG2 participate in vesicular transport and cell migration. The results will improve our understanding of diseases caused by dysfunction in small GTPases and their regulators, and may provide insights for therapeutic strategies.
Awards
2009 Outstanding Paper Award, 4th Y.S. Lee Teng-Tai Medical Science and Technology Award, Yung Shin Lee Teng-Tai Medical and Pharmaceutical Foundation
2008 Excellent Thesis/Publication Award (Ph.D. level), National Taiwan University College of Medicine
2007 Excellent Poster Presentation Award, 15th Symposium on Advances in Cell and Molecular Biology, Taiwan Society for Cell and Molecular Biology
2003 Excellent Poster Presentation Award, 11th Symposium on Advances in Cell and Molecular Biology, Taiwan Society for Cell and Molecular Biology
2008 Excellent Thesis/Publication Award (Ph.D. level), National Taiwan University College of Medicine
2007 Excellent Poster Presentation Award, 15th Symposium on Advances in Cell and Molecular Biology, Taiwan Society for Cell and Molecular Biology
2003 Excellent Poster Presentation Award, 11th Symposium on Advances in Cell and Molecular Biology, Taiwan Society for Cell and Molecular Biology
Publications
Others