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Chromatin and Disease pp 235–268Cite as

Aberrant Forms of Histone Acetyltransferases in Human Disease

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Part of the book series: Subcellular Biochemistry ((SCBI,volume 41))

One of the major mechanisms through which eukaryotic cells respond to developmental and environmental signals is by changing their gene expression patterns. This complex and tightly regulated process is largely regulated at the level of RNA polymerase II-mediated transcription. Within this process an important class of transcriptional regulators are the histone acetyltransferases (HATs), proteins that acetylate histones and non-histone substrates. While hyperacetylation of histones is generally associated with active genes, the effect of acetylation of nonhistone proteins varies between substrates resulting in for example alterations in (sub-nuclear) protein localization or protein stability. Given the central role of HATs in transcriptional regulation and other cellular processes, it may not be surprising that genetic alterations in the genes encoding HATs, resulting in aberrant forms of these regulatory proteins, have been linked with various human diseases, including congenital developmental disorders and various forms of cancer, including leukaemia. Here we will review mutations found in genes encoding human HATs and discuss the (putative) functional consequences on the function of these proteins. So far the lessons learned from naturally occurring mutations in humans have proven to be invaluable and recapitulating such genetic alterations in various experimental systems will extend our knowledge even further. This seems particularly relevant given the wide range of diseases in which acetyltransferases have been implicated and may help to open up new therapeutic avenues

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Authors and Affiliations

  1. Department of Metabolic and Endocrine Diseases, UMC Utrecht, Lundlaan 6, 3584 EA, Utrecht, The Netherlands

    Olivier Van Beekum & Eric Kalkhoven

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  1. Olivier Van Beekum
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  2. Eric Kalkhoven
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Editors and Affiliations

  1. Jawaharlal Centre for Advanced Scientific Research, Jakkur, Bangalore, India

    Tapas K. Kundu

  2. Queens College,City University of New York, New York, USA

    R. Bittman

  3. Saha Institute of Nuclear Physics, Calcutta, India

    D. Dasgupta

  4. Max-Planck-Institute for Biochemistry, Munich, Germany

    H. Engelhardt

  5. MOLISA GmbH, Magdeburg, Germany

    L. Flohe

  6. German Cancer Research Center, Heidelberg, Germany

    H. Herrmann

  7. Texas A & M University, Texas, USA

    A. Holzenburg

  8. National University of Ireland, Galway, Ireland

    H-P. Nasheuer

  9. The Hebrew University, Jerusalem, Israel

    S. Rottem

  10. DSM Nutritional Products Ltd, Basel, Switzerland

    M. Wyss

  11. Max-Planck-Institute for Biochemistry, Munich, Germany

    P. Zwickl

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Beekum, O.V., Kalkhoven, E. (2007). Aberrant Forms of Histone Acetyltransferases in Human Disease. In: Kundu, T.K., et al. Chromatin and Disease. Subcellular Biochemistry, vol 41. Springer, Dordrecht. https://doi.org/10.1007/1-4020-5466-1_11

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