Chuan He

Chuan He

Professor Chuan He
Born (1972-02-25) 25 February 1972
Guizhou, China
Fields Chemical Biology, Genetics
Institutions The University of Chicago
Alma mater University of Science and Technology of China (B.S.)
Massachusetts Institute of Technology (Ph.D.)
Doctoral advisor Stephen J. Lippard
Other academic advisors Gregory L. Verdine
Known for Epigenetics, DNA Methylation
Notable awards Searle Scholar Award (2003)
Beckman Young Investigators Award (2005)

Chuan He (simplified Chinese: 何川) (born February 25, 1972) is a Chinese-American chemical biologist, and is currently the John T. Wilson Distinguished Service Professor and Director of the Institute for Biophysical Dynamics at The University of Chicago, and an Investigator of the Howard Hughes Medical Institute.[1] Chuan He is best known for his work in discovering and deciphering reversible RNA methylation in post-transcriptional gene expression regulation.[2]

Education

He attended the University of Science and Technology of China and graduated with a B.S. in Chemistry in 1994. After his Ph.D. training with Professor Stephen J. Lippard at Massachusetts Institute of Technology, he worked with Professor Gregory L. Verdine as a Damon Runyon Postdoctoral Fellow at Harvard University. He started his independent career in the Department of Chemistry at the University of Chicago in 2002.[3]

Research

In 2010, He proposed that RNA modifications could be reversible and may have regulatory roles analogous to well-known reversible DNA and protein modifications.[2] He and colleagues subsequently discovered the first RNA demethylase that oxidatively reverses N6-methyladenosine (m6A) methylation in mammalian messenger RNA (mRNA) in 2011.[4] The existence of m6A in mRNA was discovered in 1974 in both eukaryotic and viral mRNAs; however, the biological significance and functional role were not known before He’s work. This methylation is the most abundant internal modification in mammalian mRNA. In 2012, two independent studies reported transcriptome-wide mapping of m6A in mammalian cells and tissues,[5][6] revealing a unique distribution pattern. He and co-workers identified and characterized the direct reader proteins for m6A, which impact the stability and the translation efficiency of m6A-modified mRNA, elucidating functional roles of mRNA methylation.[7][8] He’s group also purified the methyltransferase complex that mediates this methylation.[9]

The He laboratory also studies DNA methylation. He invented TAB-seq, a method that can map 5-hydroxymethylcytosine (5hmC) at base-resolution genome-wide, as well as hmC-Seal, a method that covalently labels 5hmC for its detection and profiling.[10][11] Together with two other research groups, He and co-workers have revealed the DNA N6-methyldeoxyadenosine as a new methylation mark that could affect gene expression in eukaryotes.[12][13][14]

References

  1. ↑ Chuan He Profile at the Howard Hughes Medical Institute hhmi.org Retrieved 07-28-2015
  2. 1 2 He C (November 2010). "Grand Challenge Commentary: RNA epigenetics?". Nat. Chem. Biol. 6 (12): 863–865. doi:10.1038/nchembio.482.
  3. ↑ Chuan He Faculty Page at UC Berkeley chemistry.uchicago.edu Retrieved 07-28-2015
  4. ↑ Jia G, Fu Y, Zhao X, Dai Q, Zheng G, Yang Y, Yi C, Lindahl T, Pan T, Yang YG, He C (December 2011). "N6-Methyladenosine in nuclear RNA is a major substrate of the obesity-associated FTO". Nat. Chem. Biol. 7 (12): 885–7. doi:10.1038/nchembio.687. PMC 3218240. PMID 22002720.
  5. ↑ Dominissini D, Moshitch-Moshkovitz S, Schwartz S, Salmon-Divon M, Ungar L, Osenberg S, Cesarkas K, Jacob-Hirsch J, Amariglio N, Kupiec M, Sorek R, Rechavi G (May 2012). "Topology of the human and mouse m6A RNA methylomes revealed by m6A-seq". Nature 485 (7397): 201–6. Bibcode:2012Natur.485..201D. doi:10.1038/nature11112. PMID 22575960.
  6. ↑ Meyer KD, Saletore Y, Zumbo P, Elemento O, Mason CE, Jaffrey SR (May 2012). "Comprehensive Analysis of mRNA Methylation Reveals Enrichment in 3' UTRs and near Stop Codons". Cell 149 (7): 1635–46. doi:10.1016/j.cell.2012.05.003. PMC 3383396. PMID 22608085.
  7. ↑ Wang X, Lu Z, Gomez A, Hon GC, Yue Y, Han D, Fu Y, Parisien M, Dai Q, Jia G, Ren B, Pan T, He C (January 2014). "N6-Methyladenosine-dependent regulation of messenger RNA stability.". Nature 505 (7481): 117–120. Bibcode:2014Natur.505..117W. doi:10.1038/nature12730. PMC 3877715. PMID 24284625.
  8. ↑ Wang X, Zhao BS, Roundtree IA, Lu Z, Han D, Ma H, Weng X, Chen K, Shi H, He C (June 2015). "N6-methyladenosine modulates messenger RNA translation efficiency.". Cell 161 (6): 1388–1399. doi:10.1016/j.cell.2015.05.014.
  9. ↑ Liu J, Yue Y, Han D, Wang X, Fu Y, Zhang L, Jia G, Yu M, Lu Z, Deng X, Dai Q, Chen W, He C (2014). "A METTL3-METTL14 complex mediates mammalian nuclear RNA N6-adenosine methylation". Nat. Chem. Biol. 10 (2): 93–95. doi:10.1038/nchembio.1432.
  10. ↑ Yu M, Hon GC, Szulwach KE, Song CX, Zhang L, Kim A, Li XK, Dai Q, Shen Y, Park B, Min JH, Jin P, Ren B, He C (June 2012). "Base-resolution analysis of 5-hydroxymethylcytosine in the mammalian genome.". Cell 149 (6): 1368–1380. doi:10.1016/j.cell.2012.04.027.
  11. ↑ Song CX, Szulwach KE, Fu Y, Dai Q, Yi C, Li X, Li Y, Chen CH, Zhang W, Jian X, Wang J, Zhang L, Looney TJ, Zhang B, Godley LA, Hicks LM, Lahn BT, Jin P, He C (2011). "Selective chemical labeling reveals the genome-wide distribution of 5-hydroxymethylcytosine". Nat. Biotechnol. 29 (1): 68–72. doi:10.1038/nbt.1732.
  12. ↑ Fu Y, Luo GZ, Chen K, Deng X, Yu M, Han D, Hao Z, Liu J, Lu X, Doré LC, Weng X, Ji Q, Mets L, He C (May 2015). "N6-methyldeoxyadenosine marks active transcription start sites in chlamydomonas.". Cell 161 (4): 879–892. doi:10.1016/j.cell.2015.04.010.
  13. ↑ Greer EL, Blanco MA, Gu L, Sendinc E, Liu J, Aristizábal-Corrales D, Hsu CH, Aravind L, He C, Shi Y (May 2015). "DNA methylation on N6-adenine in C. elegans.". Cell 161 (4): 868–878. doi:10.1016/j.cell.2015.04.005.
  14. ↑ Zhang G, Huang H, Liu D, Cheng Y, Liu X, Zhang W, Yin R, Zhang D, Zhang P, Liu J, Li C, Liu B, Luo Y, Zhu Y, Zhang N, He S, He C (May 2015). "N6-methyladenine DNA modification in Drosophila.". Cell 161 (4): 893–906. doi:10.1016/j.cell.2015.04.018.

External links

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