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Unexpected discovery opens up new opportunities for targeting cancer

Date:
January 10, 2012
Source:
University of Leicester
Summary:
Scientists have opened up a whole new approach to the therapeutic intervention for a family of anti-cancer drug targets, thanks to a completely new and unexpected finding.

The atomic resolution structure of histone deacetylase 3 (dark grey surface), the corepressor SMRT (light grey sticks/ribbons) and the key signalling molecule IP4 (green / orange sticks).
Credit: Image courtesy of University of Leicester

Scientists at the University of Leicester have opened up a whole new approach to the therapeutic intervention for a family of anti-cancer drug targets, thanks to a completely new and unexpected finding.

Professor Schwabe and his colleagues, Drs Watson, Fairall and Santos, have published their research this week in journal Nature detailing a new understanding of how transcriptional repression complexes work. Their work, which is based around determining atomic resolution structures of medically important bio-molecular complexes, has been ongoing for six years, and is currently funded through a £1.4 million grant from The Wellcome Trust.

Transcriptional regulatory complexes play an important role in the regulation of development, differentiation, cancer and homeostasis. Transcription is the process of creating a complementary RNA copy of a sequence of DNA and is the first step in the process of gene expression.

Professor John Schwabe, of the University of Leicester's Department of Biochemistry, said: "We have discovered a completely new and unexpected link between inositol phosphate signalling (in this case IP4) and the regulation of histone deacetylase enzymes and hence transcriptional repression or gene silencing.

"In simple terms, we have shown that IP4 acts as a natural signalling molecule to regulate histone deacetylase enzymes which play a key role in regulating gene expression. Apart from the considerable intellectual importance of understanding how transcription is regulated, repression complexes are important therapeutic targets for a number of cancers including several types of leukemia.

"Our research identifies several new means to potentially target histone deacetylase enzymes therapeutically: either by using drugs to prevent IP4 binding to the enzyme or by interfering with the pathway through which the body makes IP4. Thus this work opens up a whole new area of research with potential for new drugs and a new approach to targeting histone deacetylase enzymes."

Professor Schwabe said that this research is not only an exciting breakthrough in the field, but is also a technological feat relying on both the excellent research facilities in Leicester and the microfocus X-ray source at the Diamond Light Source in Oxfordshire.


Story Source:

The above story is based on materials provided by University of Leicester. Note: Materials may be edited for content and length.


Journal Reference:

  1. Peter J. Watson, Louise Fairall, Guilherme M. Santos, John W. R. Schwabe. Structure of HDAC3 bound to co-repressor and inositol tetraphosphate. Nature, 2012; DOI: 10.1038/nature10728

Cite This Page:

University of Leicester. "Unexpected discovery opens up new opportunities for targeting cancer." ScienceDaily. ScienceDaily, 10 January 2012. <www.sciencedaily.com/releases/2012/01/120110140233.htm>.
University of Leicester. (2012, January 10). Unexpected discovery opens up new opportunities for targeting cancer. ScienceDaily. Retrieved August 21, 2014 from www.sciencedaily.com/releases/2012/01/120110140233.htm
University of Leicester. "Unexpected discovery opens up new opportunities for targeting cancer." ScienceDaily. www.sciencedaily.com/releases/2012/01/120110140233.htm (accessed August 21, 2014).

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