Home Site Map Chinese
Dr. Fu Huang
Assistant Research Fellow
Room 612, Institute of Biological Chemistry, Academia Sinica
128, Academia Road Sec. 2, Nankang, Taipei 115, Taiwan
TEL: +886-2-27855696 ext. 6120
FAX: +886-2-27889759

Post-translational modification (PTM) on histones plays important roles in regulating all DNA-dependent processes, including transcription and replication, by modulating the accessibility of DNA and recruiting protein factors to chromatin. PTMs on histones include phosphorylation, ubiquitination, ADP-ribosylation, O-GlcNAcylation, methylation and acetylation. The acetylation of lysine residues in histones is catalyzed by enzymes called histone acetyltransferases (HATs). Other than histones, many non-histone substrates have also been identified for HATs, adding another layer of complexity to their biological roles. Our lab is interested in understanding the functions of HATs and the mechanisms underlying their roles, and we are currently focusing on the Drosophila HAT Enok. Enok is a homolog of human MOZ, a key regulator of hematopoiesis and involved in leukemia, and is important for neuroblast proliferation and stem cell maintenance. Given that the protein complexes formed by Enok/MOZ are highly conserved between Drosophila and human, we are interested in using Drosophila as a simple and great genetic model to dissect the regulations and roles of Enok/MOZ.

Currently, we are pursuing two topics:
1. The roles of Enok in cell cycle regulation through acetylating non-histone targets.
2. The transcriptional roles of Enok in germline stem cell maintenance.

2005 - 2011 Ph.D., Biochemistry, Vanderbilt University School of Medicine
2001 - 2005 B.S., Life Science, National Tsing Hua University

2015,11 - present Assistant Research Fellow, Institute of Biological Chemistry, Academia Sinica
2011 - 2015 Postdoctoral Research Associate, Stowers Institute for Medical Research

    Publications List
Regulation of KAT6 acetyltransferases and their roles in cell cycle progression, stem cell maintenance, and human disease. (invited review)
Huang F, Abmayr SM, Workman JL Mol Cell Biol (2016)
The Enok acetyltransferase complex interacts with Elg1 and negatively regulates PCNA unloading to promote the G1/S transition. (cover article)
Huang F, Saraf A, Florens L, Kusch T, Swanson SK, Szerszen LT, Li G, Dutta A, Washburn MP, Abmayr SM, Workman JL Genes Dev (2016)
Interaction of the Jhd2 H3K4 demethylase with chromatin is promoted by histone H2A surfaces and restricted by H2B ubiquitylation.
Huang F, Ramakrishnan S, Pflueger C, Parnell TJ, Kasten MM, Currie SL, Bhachech N, Horikoshi M, Graves BJ, Bhaskara S, Cairns BR, Chandrasekharan MB J Biol Chem (2015)
Histone acetyltransferase Enok regulates oocyte polarization by promoting expression of the actin nucleation factor spire.
Huang F, Paulson A, Dutta A, Venkatesh S, Smolle M, Abmayr SM, Workman JL Genes Dev (2014)
Directing transcription to the right way.
Huang F, Workman JL Cell Res (2013)
Decoding the trans-histone crosstalk: methods to analyze H2B ubiquitination, H3 methylation and their regulatory factors.
Chandrasekharan MB, Huang F, Sun ZW Methods (2011)
Histone H2B C-terminal helix mediates trans-histone H3K4 methylation independent of H2B ubiquitination.
Chandrasekharan MB, Huang F, Chen YC, Sun ZW Mol Cell Biol (2010)
Histone H2B ubiquitination and beyond: Regulation of nucleosome stability, chromatin dynamics and the trans-histone H3 methylation.
Chandrasekharan MB, Huang F, Sun ZW Epigenetics (2010)
The JmjN domain of Jhd2 is important for its protein stability and the PHD finger mediates its chromatin association independent of H3K4 methylation.
Huang F, Chandrasekharan MB, Chen YC, Bhaskara S, Hiebert SW, Sun ZW J Biol Chem (2010)
Ubiquitination of histone H2B regulates chromatin dynamics by enhancing nucleosome stability.
Chandrasekharan MB, Huang F, Sun ZW Proc Natl Acad Sci U S A (2009)

Updated 2018.08.01

Browser & IE Recommendations: 1024*768 / IE 8.0、Firefox 10.0

128, Academia Road Sec. 2, Nankang, Taipei 115, Taiwan Tel : 886-2-27855696 Fax : 886-2-27889759

Copyright © 2013.01 IBC, Academia Sinica. All rights reserved.    Terms of use