Woojin AnAssistant Professor
Biochemistry & Molecular Biology, Norris Comprehensive Cancer Center
Keck School of Medicine |  | |
| Send E-mail to: woojinan@usc.edu | | | Telephone: 323-442-4398 | Fax: 323-442-4433 | | Office: NRT 6507 | Mail Code: 9601 HSC |
Education:
PhD 1998 Biochemistry - Oregon State University, Corvallis, Oregon
Postdoctoral Research Fellowship:
1998 - 2004 The Rockefeller University
Started at USC: 2004 Research Topics: Gene Regulation/Transcription, Cancer Cell Biology, Signal Transduction, Protein Chemistry/Enzymology, Epigenetics
Research Description
In human cells, the DNA is compacted into the nucleus as a complex structure known as chromatin. The basic repeating unit of chromatin is the nucleosome, which consists of 146 bp of DNA wrapped around a core histone octamer containing pairs of each of the histone proteins, H2A, H2B, H3 and H4. All DNA-dependent processes within this chromatin context require remodeling activities that counterbalance the repressive nature of chromatin. Two major remodeling processes are post-translational modifications of histone N-terminal domains (e.g., acetylation, methylation, phosphorylation and ubiquitination) and exchange of histone variants (e.g., H2A.Z, H2AX, macroH2A, H2A-Bbd, H3.3 and CENP-A) into and out of chromatin.
Our long-term goal is to understand how histone modifications and variants, via activation or repression of specific genes, regulate critical cellular events to attenuate various cellular malignancies, notably cancer development. To investigate these aspects, we have established powerful protocols to interrogate the cellular function of histone modifications and variants as a signal which would facilitate the recruitment/retention of gene regulation machinery at the site of transcription. Using this experimental system, current research efforts are mainly directed towards understanding how such diverse histone modifications and variants are selectively recruited to a specific gene under a distinct condition and how modified histones and incorporated variants contribute to transcriptional regulation. Once the active/repressive functions of histone modifications and variants are determined, the understanding of the mechanism of action of the identified epigenetic reprogramming in critical cellular processes will be an exciting challenge for our investigation.
10 Selected Publications:
Click here to view all the publications for this faculty
Choi J,Heo K,An W - Cooperative action of TIP48 and TIP49 in H2A.Z exchange catalyzed by acetylation of nucleosomal H2A. - Nucleic Acids Res [2009] Oct;37(18):5993-6007 PubMed
Kim H,Heo K,Kim JH,Kim K,Choi J,An W - Requirement of histone methyltransferase SMYD3 for estrogen receptor-mediated transcription. - J Biol Chem [2009] Jul 24;284(30):19867-77 PubMed
Kim JH,Yang CK,Heo K,Roeder RG,An W,Stallcup MR - CCAR1, a key regulator of mediator complex recruitment to nuclear receptor transcription complexes. - Mol Cell [2008] Aug 22;31(4):510-9 PubMed
Robinson PJ,An W,Routh A,Martino F,Chapman L,Roeder RG,Rhodes D - 30 nm chromatin fibre decompaction requires both H4-K16 acetylation and linker histone eviction. - J Mol Biol [2008] Sep 12;381(4):816-25 PubMed
Heo K,Kim H,Choi SH,Choi J,Kim K,Gu J,Lieber MR,Yang AS,An W - FACT-mediated exchange of histone variant H2AX regulated by phosphorylation of H2AX and ADP-ribosylation of Spt16. - Mol Cell [2008] Apr 11;30(1):86-97 PubMed
Kim K,Choi J,Heo K,Kim H,Levens D,Kohno K,Johnson EM,Brock HW,An W - Isolation and characterization of a novel H1.2 complex that acts as a repressor of p53-mediated transcription. - J Biol Chem [2008] Apr 4;283(14):9113-26 PubMed
Choi J,Kim B,Heo K,Kim K,Kim H,Zhan Y,Ranish JA,An W - Purification and characterization of cellular proteins associated with histone H4 tails. - J Biol Chem [2007] Jul 20;282(29):21024-31 PubMed
An W - Histone acetylation and methylation: combinatorial players for transcriptional regulation. - Subcell Biochem [2007] ;41():351-69 PubMed
Heo K,Kim B,Kim K,Choi J,Kim H,Zhan Y,Ranish JA,An W - Isolation and characterization of proteins associated with histone H3 tails in vivo. - J Biol Chem [2007] May 25;282(21):15476-83 PubMed
Doyen CM,An W,Angelov D,Bondarenko V,Mietton F,Studitsky VM,Hamiche A,Roeder RG,Bouvet P,Dimitrov S - Mechanism of polymerase II transcription repression by the histone variant macroH2A. - Mol Cell Biol [2006] Feb;26(3):1156-64 PubMed
| |
