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Faculty Profiles

Nam-On Ku

Associate Professor, Department of Integrated OMICS for Biomedical Science, Graduate School

  • Ph.D. in Microbiology, Ohio State University
  • M.S. in Biology, Yonsei University
  • B.S. in Biology, Yonsei University

Email: namonku@yonsei.ac.kr
Tel: 02-2123-2697

Profile

Previous positions: 

  • Research Assistant Professor, School of Medicine, Department of Molecular and Integrative Physiology, 
    University of Michigan
  • Senior Research Scientist, School of Medicine, Division of Gastroenterology, Stanford University
  • Postdoctoral Fellow, School of Medicine, Division of Gastroenterology, Stanford University

Education

Ph.D. in Microbology, Ohio State University 
M.S. in Biology, Yonsei University, Seoul, Korea
B.S. in Biology, Yonsei University, Seoul, Korea

Courses and Current Research Areas

Courses
 UBC2002-01-00, Cell Biology (1)
• UBC2003-01-00, Cell Biology (2)
• UBC3005-01-00, Physiology
• BIO1011-03-00, General Biology and Experiment (1)
• BIO1012-03-00, General Biology and Experiment (2)
• OBM7012-01-00, Cell Signaling and diseases (1)
• OBM7800-01-00, Disease Phenotype in Mouse Model (1)

Research Areas
• Regulation and function of intermediate filament proteins in cell signaling
• Study of keratin mutations in transgenic mouse model
• Association of intermediate filament mutations in human diseases

Selected Publications

1) Ku N-O, and Omary MB (1994).  Identification of the major physiologic phosphorylation site of human keratin 18: potential kinases and a role in filament reorganization. J Cell Biol 117:161-171.
2) Ku N-O, Michie S, Oshima RG, and Omary MB (1995). Chronic hepatitis, hepatocyte fragility and increased soluble phosphoglycokeratins in transgenic mice expressing a keratin 18 conserved arginine mutant. J Cell Biol 131:1303-1314.
3) Ku N-O, Michie SA, Soetikno RM, Resurreccion EZ, Broome RL, Oshima RG, and Omary MB (1996).  Susceptibility to hepatotoxicity in transgenic mice that express a dominant-negative human keratin 18 mutant.  J Clin Invest 98:1034-1046.
4) Ku N-O, Wright TL, Terrault NA, Gish R, and Omary MB (1997).  Mutation of human keratin 18 in association with cryptogenic cirrhosis.  J Clin Invest 99:19-23.
5) Ku N-O, Liao J, and Omary MB (1998). Phosphorylation of human keratin 18 serine-33 regulates binding to 14-3-3 proteins.  EMBO J 17:1892-1906.
6) Ku N-O, Michie SA, Soetikno RM, Resurreccion EZ, Broome RL, and Omary MB (1998). Mutation of a major keratin phosphorylation site predisposes to hepatotoxic injury in transgenic mice. J Cell Biol 143:2023-2032.
7) Ku N-O, and Omary MB (2000).  Keratins turn over by ubiquitination in a phosphorylation-modulated fashion.  J Cell Biol 149:547-552.
8) Ku N-O, Gish R, Wright TL, and Omary MB (2001). Keratin 8 mutations in patients with cryptogenic liver disease.  N Engl J Med 344:1580-1587.
9) Ku N-O, Michie SA, Resurreccion EZ, Broome RL. and Omary MB  (2002).  Keratin binding to 14-3-3 proteins modulates keratin filaments and hepatocyte mitotic progression.  Proc Natl Acad Sci USA 99:4373-4378.
10) Ku N-O, Soetikno RM, and Omary MB (2003).  Keratin mutation in transgenic mice predisposes to FAS but not TNF induced apoptosis and massive liver injury. Hepatology 37:1006-1014.
11) Ku N-O, Darling J, Krams SM, Esquivel CO, Keeffe EB, Sibley RK, Lee YM, Wright TL and Omary MB (2003). Keratin 8 and 18 mutations are risk factors for developing liver disease of multiple etiologies. Proc Natl Acad Sci USA 100:6063-6068.
12) Ku N-O, Fu H, and Omary MB (2004).  Raf-1 activation disrupts its binding to keratins during cell stress. J Cell Biol 166:479-485.
13) Ku N-O, Lim JK, Krams SM, Esquivel CO, Keeffe EB, WrightTL, Parry D and Omary MB (2005).  Keratins as susceptibility genes for end-stage liver disease. Gastroenterology 129:885-893.
14) Omary MB, Ku N-O, Tao G-Z, Toivola DM, and Liao J (2006).  'Heads and tails' of intermediate filament phosphorylation: multiple sites and functional insights. Trends Biochem Sci. 31:383-394.
15) Ku N-O, and Omary MB (2006).  A disease and phosphorylation related non-mechanical function for keratin 8. J Cell Biol 174:115-125.
16) Omary MB, and Ku N-O (2006).  Cell biology: skin care by keratins. Nature 441:296-297.
17) Harada M, Strnad P, Resurreccion EZ, Ku N-O, and Omary MB (2007).  Keratin 18 overexpression but not phosphorylation or filament organization blocks mouse Mallory body formation.  Hepatology 45:88-96.
18) Ku N-O, Strnad P, Zhong B, Tao G-Z, and Omary MB (2007).  Keratins let liver live: mutations predispose to liver disease and crosslinking generates Mallory-Denk bodies.  Hepatology 46:1639-1649.
19) Omary MB, Ku N-O, Strnad P, Zhong B, Tao G-Z, and Toivola DM (2009).  Towards unraveling the complexity of simple epithelial keratins in human disease.  J Clin Invest 119:1794-1805.
20) Ku N-O, Toivola DM, Strnad P, and Omary MB. Cytoskeletal keratin glycosylation protects from epithelial tissue injury (2010). Nat Cell Biol 12:876-885.
21)  Zhou Q, Snider NT, Liao J, Li DH, Hong A, Ku N-O, Cartwright CA, and Omary MB (2010).  Characterization of in vivo keratin 19 phosphorylation on tyrosine-391. PLoS One 5:e13538.
22) Strnad P, Paschke S, Jang KH, and Ku N-O (2012). Keratins: markers and modulators of liver disease. Curr Opin Gastroenterol. 28:209-16.
23) Lee J, Jang KH, Kim H, Lim Y, Kim S, Yoon HN, Chung IK, Roth J, and Ku N-O (2013). Predisposition to apoptosis in keratin 8-null liver is related to inactivation of NF-κB and SAPKs but not decreased c-Flip. Biology Open 2:695-702.
24) Yi H, and Ku N-O (2013). Intermediate filaments of the lung. Histochem Cell Biol. 140:65-69.
25) Weerasinghe SV*, Ku N-O*, Altshuler PJ, Kwan R, and Omary MB (2014). Mutation of keratin 18 caspase digestion sites interferes with filament reorganization and promotes hepatocyte leakiness and necrosis. J Cell Sci. 127:1464-1475
26) Ku N-O, Strnad P, Bantel H, and Omary MB (2016). Keratins: Biomarkers and modulators of apoptotic and necrotic cell death in the liver. Hepatology 64:966-976
27) Yoon HN, Yoon SY, Hong JH, and Ku N-O (2017). A mutation in keratin 18 that causes caspase-digestion resistance protects homozygous transgenic mice from hepatic apoptosis and injury. J Cell Sci.130:2541-2550.

More Information

Patent
Keratin 8 and 18 mutations are risk factors for developing liver disease of multiple etiologies (MB Omary and N-O Ku): patent#, US 7838217 B1; date of patent, Nov 23, 2010

International Oral Presentations
1) Ku N-O, Fu H, and Omary MB. Keratin 8 associates with and sequesters Raf kinase during interphase in a phosphorylation-dependent fashion. Gordon Research Conference: Intermediate Filaments, US, Aug. 2002.
2) Ku N-O, Darling JM, Wright TL, Krams SM, and Omary MB. Keratin mutations predispose to cryptogenic and noncryptogenic liver disease. American Gastroenterological Association Conference: Digestive Disease Meeting, US, May 2002.
3) Ku N-O, Darling JM, Krams SM, Esquivel CO, Keeffe EB, Wright TL, and Omary MB. A new and highly prevalent keratin mutation in patients with liver disease. American Gastroenterological Association Conference: Digestive Disease Meeting, US, May 2003.
4) Ku N-O, Fu H, and Omary MB. Keratins as modulators of 14-3-3 proteins and vice versa. Gordon Research Conference: Biology of 14-3-3 Proteins, US, Feb. 2004.
5) Ku N-O, Lim JK, Krams SM, Esquivel CO, Keeffe EB, Wright TL, Parry D, and Omary MB. Keratins as susceptibility genes for liver disease. American Gastroenterological Association Conference: Digestive Disease Meeting, US, May 2004.
6) Ku N-O, Lim JK, Krams SM, Esquivel CO, Keeffe EB, Wright TL, Parry D, and Omary MB. Keratins as susceptibility genes for liver disease. Gordon Research Conference: Intermediate Filaments, US, Aug. 2004.
7) Ku N-O, and Omary MB.  Human cirrhosis-associated keratin-8 glycine61-to-cysteine mutation predisposes to liver injury in transgenic mice.  American Gastroenterological Association Conference: Digestive Disease Meeting, US, May 2005.
8) Ku N-O, and Omary MB.  Keratin-8 mutation predisposes to liver injury by altering stress kinase-mediated phosphorylation.  American Society for Cell Biology Meeting, US, Dec. 2005.
9) Ku N-O, Toivola DM, Strnad P and Omary MB.  A new functional role for keratin 18 glycosylation in protection from injury in epithelial tissues.  American Society for Cell Biology Meeting, Dec. 2007.
10) Ku N-O. In vivo significance of keratin glycosylation in liver injury. ACGG (Asian Communications of Glycobiology and Glycotechnology) Conference, Taiwan, Oct. 2010.
11) Ku N-O. Epithelial keratin-associated disease. Gordon Research Conference: Intermediate Filaments, US, June 2012.
12) Ku N-O. Function of keratins in lung. Joint symposium of Society for Histochemistry and COST Nanonet Action, Czech Republic, June 2013.

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