최철용 교수님(Cheol Yong Choi)
페이지 정보
작성일 21-04-27 17:26본문
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최철용 (Cheol Yong Choi) |
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직함 |
교수 (자연대학장) |
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전공 |
분자유전학 |
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연구실 |
분자유전학연구실 |
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전화 |
031-290-7010 |
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사무실 |
제2과학관 32205 |
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이메일 |
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| 연구실 소개 |
연구 분야:분자유전학 실험실에서는 암세포의 발암 과정과 암세포 전이 과정에서 일어나는 신호 전달 기전을 연구하고 이를 이용하여 새로운
신약후보물질 발굴 및 응용 방안을 찾는 연구를 하고 있습니다.
응용 분야 또는 산물(product):암 환자에서 돌연변이가 일어나거나 과발현이 일어나 있는 새로운 단백질을 발견하면 그 단백질을 제어할 수
있는 새로운 항암 후보물질로 개발할 수 있습니다. 또한 자연계에 존재하는 natural product가 항암효과를 가지는지도 분석할 수 있습니다.
산학협력 사례 또는 취업 분야:저희 연구실은 벤처 회사와 공동 연구를 통해 개발 중인 신약의 성질을 규명하는 연구를 수행하고 있습니다.
저희 연구실을 졸업한 학생들은 삼성바이오로직스, 삼성바이오에피스, 셀트리온, 종근당, 일동제약, 식약처 등과 같은 바이오 관련 및 제약회사
에서 다양한 업무를 맡아서 일을 하고 있습니다.
| Research Background |
Signal transduction pathways regulate many different aspects of cellular metabolism, function and development. Recently many components of each
signaling pathway were identified and characterized as important molecules to understand several cancers and genetic diseases. Protein phosphorylation and dephosphorylation is one of the major mechanisms of signal integration in eukaryotic cells. It can be achieved through the phosphorylation of proteins that control the levels of second messengers, through the phosphorylation of protein kinases and phosphatases themselves, or through the reversible phosphorylation of their substrates. The family of homeodomain interacting protein kinases (HIPKs) consists of four related kinases termed HIPK1 to HIPK4. HIPKs function as a switchboard regulating the transcriptional machinery, development, differentiation and cell death (Fig. 1). In response to DNA damage, cells have to decide between different cell fate programs. Activation of the tumor suppressor HIPK2 specifies the DNA damage response and tips the cell fate balance between DNA repair and apoptotic response. Our recent work has identified HIPK2 as a regulator of the initiation and termination of DNA repair in response to ionizing radiation (Fig. 2). Furthermore, HIPK2 triggers apoptosis through regulatory phosphorylation of a set of cellular key molecules including the tumor suppressor p53 and CtBP (Fig. 3). A number of conditions representing precarious situations such as DNA damage, hypoxia, reactive oxygen intermediates and metabolic stress affect the function of HIPKs. The kinases function as integrators for these stress signals and feed them into many different downstream effector pathways that serve to cope with these precarious situations. Their central role as signaling hubs with the ability to shape many downstream effector pathways frequently implies them in proliferative diseases such as cancer, neurodegenerative disease and fibrosis (Fig. 4). So we have interested in the deciphering molecular networks of signaling pathway particularly associated with human diseases such as cancer, diabetes, neurodegenerative disease.
Figure 1. HIPKs function as a switchboard regulating various physiological responses
Figure 2. HIPK2-mediated regulation of DNA repair in response to IR
Figure 3. HIPK2 stabilization and PML-NB targeting for p53 activation and apoptosis
Figure 4. HIPK1 is highly expressed in primary lung tumors
| Peer review paper |
- Kim HN, Seo JS, Bang J, Kim EA, Sung KS, Yoon SJ, Yun H, Yoo HY, Choi CY (2014) Covalent conjugation of Nuclear mitotic apparatus protein (NuMA) with SUMO-1 in a cell cycle-dependent manner. Biochem. Biophy. Res. Comm. 443(1):259-265.
- Hwang J, Lee SY, Choi JR, Shin KS, Choi CY, Kang SJ (2013) SIRT1 negatively regulates the protein stability of HIPK2. Biochem. Biophy. Res. Comm. 441(4):799-804.
- Kim SJ, Ahn JW, Kim H, Ha HJ, Lee SW, Kim HK, Lee SH, Hong HS, Kim YH, and Choi CY (2013) Two -strands of RAGE participate in the recognition and transport of amyloid- peptide across the blood brain barrier. Biochem. Biophy. Res. Comm. 394(4):966-971.
- Choi DW, Na WJ, Kabir MH, Yi EB, Kwon SJ, Yeom JH, Seo KY, Ahn JW, Choi HH, Lee YH, Shin MK, Park SH, Yoo HY, Isono K-I, Koseki H, Kim ST, Lee CJ, Kim YH, and Choi CY (2013) WIP1, a Homeostatic Regulator of the DNA Damage Response, Is Targeted by HIPK2 for Phosphorylation and Proteasomal Degradation. Molecular Cell 51, 1-12.
- Yoo YD, Han DH, Jang JM, Zakrzewska A, Kim SY, Choi CY, Lee YJ and Kwon YT (2013) Molecular Characteristics of Cancer Stem-like Cells Derived from Human Breast Cancer Cells. Anticancer Research 33(3): 763-777.
- Lee D, Park SJ, Sung KS, Park J, Lee SB, Park SY, Lee HJ, Ahn JW, Choi SJ, Lee SG, Kim SH, Kim DH, Kim J, Kim Y, Choi CY. (2012) Mdm2 associates with Ras effector NORE1 to induce the degradation of oncoprotein HIPK1. EMBO Rep. 13(2): 163-169.
- Sung KS, Lee Y-A, Kim ET, Lee S-R, Ahn J-H, Choi CY (2011) Role of the SUMO-interacting motif in HIPK2 targeting to the PML nuclear bodies and regulation of p53. Exp. Cell Res. 317, 1060-1070.
- Ryu SY, Do SH, Chung JY, Kim TH, Kim SH, Choi CY, Jeong KS, Park SJ (2011) Activation of MAP kinases during progression of radiation-induced pneumonitis in rats. Hum. Exp. Toxicol. 30(8):876-883.
- Kim JH, Sung KS, Jung SM, Lee YS, Kwon JY, Choi CY, Park SH (2011) Pellino-1, an adaptor protein of interleukin-1 receptor/toll-like receptor signaling, is sumoylated by Ubc9. Mol Cells 31(1):85-89.
- Kim HG, Ahn JW, Kurth I, Ullmann R, Kim HT, Kulharya A, Ha KS, Itokawa Y, Meliciani I, Wenzel W, Lee D, Rosenberger G, Ozata M, Bick DP, Sherins RJ, Koga H, Nagase T, Kim SH, Kim CH, Ropers HH, Gusella JF, Kalscheuer V, Choi CY, Layman LC (2010) WDR11, a WD protein that interacts with transcription factor EMX1, is mutated in idiopathic hypogonadotropic hypogonadism and Kallmann syndrome. Am. J. Human Genet. 87(4): 465-479.
- Kim Y, Song YB, Kim TY, Kim I, Han SJ, Ahn Y, Cho SH, Choi CY, Chay KO, Yang SY, Ahn BW, Huh WK, Lee SR (2010) Redox regulation of the tumor suppressor PTEN by glutathione. FEBS Lett. 584(16) 3550-3556.
- Oh W, Lee EW, Lee D, Yang MR, Ko A, Yoon CH, Lee HW, Bae YS, Choi CY, Song J. (2010) Hdm2 negatively regulatestelomerase activity by functioning as an E3 ligase of hTERT. Oncogene 394(4):966-971.
- Jin Z, Kim YJ, Park Y-K, Choi YD, Lee JH, Lee D, Choi CY, Juhng S-W and Choi C. (2010) Type 3 Repeats of Thrombospondin-2 Increases Metastasis in Mouse Colorectal Cancer CT-26 Cells. Chonnam Medical Journal 46 (1): 7-18.
- Kim EA, Kim JE, Sung KS, Choi DW, Lee BJ, Choi CY (2010) Homeodomain-interacting protein kinase 2 (HIPK2) targets b-catenin for phosphorylation and proteasomal degradation. Biochem. Biophy. Res. Comm. 394(4):966-971.
- Lee EK, Lee YS, Lee H, Choi CY, Park SH (2009) 14-3-3epsilon protein increases matrix metalloproteinase-2 gene expression via p38 MAPK signaling in NIH3T3 fibroblast cells. Exp Mol Med. 41(7):453-561.
- Kim SY, Choi DW, Kim EA, and Choi CY (2009) Stabilization of HIPK2 by escape from proteasomal degradation mediated by the E3 ubiquitin ligase Siah1. Cancer Lett. 279(2):177-184.
- Ahn JW, Lee YA, Ahn JH, and Choi CY (2009) Covalent conjugation of Groucho with SUMO-1 modulates its corepressor activity. Biochem. Biophy. Res. Comm. 379(1):160-165.
- Zhu J, Zhu S, Guzzo CM, Ellis NA, Sung KS, Choi CY, Matunis MJ (2008) Small ubiquitin-related modifier (SUMO) binding determines substrate recognition and paralog-selective SUMO modification. J. Biol. Chem. 283, 29405-29415.
- Park S-J, Lee D, Choi CY and Ryu SY (2008) Induction of apoptosis by NORE1A in a manner dependent on its nuclear export. Biochem. Biophy. Res. Comm. 28, 56-61.
- Lee MR, Lee D, Shin SK, Kim YH, Choi CY. (2008) Inhibition of APP intracellular domain (AICD) transcriptional activity via covalent conjugation with Nedd8. Biochem. Biophys. Res. Comm. 366, 976-981.
- Choi DW, Seo YM, Kim EA, Sung KS, Ahn JW, Park SJ, Lee SR, Choi CY. (2008) Ubiquitination and degradation of homeodomain-interacting protein kinase 2 by WD40 repeat/SOCS box protein WSB-1. J. Biol. Chem. 283, 4682-4689.
- Kim EA, Noh YT, Ryu M-J, Kim H-T, Lee S-E, Kim CH, Lee C, Kim YH and Choi CY (2006) Phosphorylation and transactivation of Pax6 by Homeodomain-Interacting Protein Kinase 2. J. Biol. Chem. 281(11), 7489-7497.
- Kang HJ, Kim ET, Lee HR, Park JJ, Go YY, Choi CY and Ahn JH (2006) Inhibition of SUMO-Independent PML Oligomerization by the Human Cytomegalovirus 2 IE1 Protein. J. Gen. Virol. 87, 2181-2190.
- Youm JW, Kim H, Han JHL, Jang CH, Ha HJ, Mook-Jung I, Jeon JH, Choi CY, Kim YH, Kim HS, Joung H (2005) Transgenic potato expressing A reduce A burden in Alzheimer’s disease mouse model. FEBS Lett. 579(30) 6737-6744.
- Kim YH, Sung KS, Lee S-J, Kim Y-O, Choi CY* and Kim Y* (2005) Desumoylation of Homeodomain-Interacting Protein Kinase 2 (HIPK2) through the cytoplasmic-nuclear shuttling of the SUMO-specific protease SENP1. FEBS Lett. Nov 7;579(27):6272-6278.
- Kim H, Park BS, Lee KG, Choi CY, Jang SS, Kim YH and Lee SE (2005) Effects of Naturally Occurring Compounds on Fibril Formation and Oxidative Stress of -Amyloid. J. Agr. Food Chem. Nov 2; 53(22):8537-8541.
- Kim YH and Choi CY (2005) Homo- and Hetero-Dimerization of Homeodomain-Interacting Protein Kinases (HIPKs) Kor. J. G enet. Sep 30; 27, 195-202.
- Sung KS, Go YY, Ahn JH, Kim YH, Kim Y, Choi CY (2005) Differential interactions of the homeodomain-interacting protein kinase 2 (HIPK2) by phosphorylation-dependent sumoylation. FEBS Lett. 579, 3001-3008
- Choi CY, Kim YH, Kim YO, Park SJ, Kim EA, Riemenschneider W, Gajewski K, Schulz RA, Kim Y. (2005) Phosphorylation by the DHIPK2 protein kinase modulates the corepressor activity of Groucho. J. Biol. Chem. 280, 21427-21436.
- Lee HR,Kim DJ, Lee JM, Choi CY, Ahn BY, Hayward GS, and Ahn JH. (2004) Ability of the human cytomegalovirus IE1 protein to modulate sumoylation of PML correlates with its functional activities in transcriptional regulation and infectivity in cultured fibroblast cells. J. Virol. 78, 6527-6542.
- Kim J-R, Lee S-M, Cho S-H, Kim J-H, Kim B-H , Kwon J, Choi CY, Kim Y-D, and Lee S-R (2004) Oxidation of thioredoxin reductase in HeLa cells stimulated with tumor necrosis factor-. . FEBS Letters 567, 189-196.
- Lee J-M, Kang H-J, Lee H-R, Choi CY, Jang W-J, and Ahn J-H (2003) PIAS1 enhances SUMO-1 modification and the transactivation activity of the major immediate-early IE2 protein of human cytomegalovirus. FEBS Letters 555, 322-328
| Funding history |
| • 2011 - 2014 | Ubl 표적발굴 및 결합효소, 유리효소, 표적단백질의 작용기전. 교육과학기술부 |
| • 2011 - 2014 | 프로모터 메틸화에 의한 발암과정에서 HIPK1 oncoprotein의 기능연구. 보건복지부 |
| • 2009 - 2012 | DNA 손상인지 및 신호전달 조절연구. 교육과학기술부 |
| • 2009 - 2012 | 세포증식과 DNA손상의 센서기능을 하는 인 단백질의 조절 연구. 교육과학기술부 |
| • 2009 - 2011 | 백혈병환자에서 발견되는 HIPK2 mutant에 의한 급성골수성 백혈병 발암기전 연구. 보건복지부 |
| • 2006 - 2009 | 암 억제인자 HIPK2를 활용한 대장암 제어기술. 교육과학기술부 |
| • 2006 - 2009 | 발생과 분화과정에서 세포사멸 억제 단백질의 기능연구. 교육과학기술부 |
| • 2002 - 2005 | Oncogenic transformation 에서 nuclear cofactor complex의 기능. 교육과학기술부 |
| • 2002 - 2004 | HIPK2에 의한 Pax6 인산화에 따른 전사활성 연구. 교육과학기술부 |
| • 2002 - 2005 | 세포분화 과정에서 HIPK2에 의한 Groucho corepressor complex의 조절기전. 교육과학기술부 |
| Education and experiences |
| • 2012 - preset | Professor, Dept. of Biological Sciences, Sungkyunkwan University |
| • 2006 - 2012 | Associate Professor, Dept. of Biological Sciences, Sungkyunkwan University |
| • 2002 - 2006 | Assistant Professor, Dept. of Biological Sciences, Sungkyunkwan University |
| • 1997 - 2001 | Postdoc., Lab. of Molecular Cardiology, National Institutes of Health, USA |
| • 1995 - 1996 | Postdoc., Research Center for Cell Differentiation, Seoul National University |
| • 1995 | Ph.D., Department of Molecular Biology, Seoul National University |
| • 1990 - 1991 | Military Service |
| • 1990 | M.S., Department of Molecular Biology, Seoul National University |
| • 1987 | B.S., Department of Zoology, Seoul National University |
| Professional activites |
| Member: | American
Society for Biochemistry and Molecular Biology, American Society for Cell
Biology, Korean Society for Molecular Cell Biology. |
| Editorial Board: | Cancer Letters, Biomed Research International, World Journal of Biochemistry. |
| Lecture |
• 유전학특론 (Special topics of Genetics): 대학원 대상, 봄 학기
• 생명과학 (General Biology): 학부 대상, 봄-가을 학기
| People |
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안장원 (Jang Won Ahn) |
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과정 |
이학박사 |
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연구실 |
분자유전학연구실 | |
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전화 |
031-290-5910 |
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사무실 |
제2과학관 32203 |
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이메일 |
kamui1110@nate.com | |
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최동욱 (Dong Wook Choi) |
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과정 |
이학박사 |
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연구실 |
분자유전학연구실 | |
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전화 |
031-290-5910 |
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사무실 |
제2과학관 32203 |
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이메일 |
cococode@hotmail.com | |
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나우주 (Woo Ju Na) |
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과정 |
박사과정 |
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연구실 |
분자유전학연구실 | |
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전화 |
031-290-5910 |
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사무실 |
제2과학관 32203 |
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이메일 |
kyrieles@naver.com | |
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김선직 (Sun Jick Kim) |
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과정 |
이학박사 |
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연구실 |
분자유전학연구실 | |
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전화 |
031-290-5910 |
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사무실 |
제2과학관 32203 |
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이메일 |
godmous79@hanmail.net | |
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함선규 (Seon Kyu Ham) |
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과정 |
석사과정 |
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연구실 |
분자유전학연구실 | |
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전화 |
031-290-5910 |
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사무실 |
제2과학관 32203 |
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이메일 |
skham05@naver.com | |
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민기홍 (Ki Hong Min) |
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과정 |
석사과정 |
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연구실 |
분자유전학연구실 | |
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전화 |
031-290-5910 |
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사무실 |
제2과학관 32203 |
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이메일 |
ajpump@naver.com | |
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서경완 (Kyoung Wan Seo) |
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과정 |
석사과정 |
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연구실 |
분자유전학연구실 | |
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전화 |
031-290-5910 |
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사무실 |
제2과학관 32203 |
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이메일 |
sko0506@naver.com | |
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