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Nonhistone targets of KAT2A and KAT2B implicated in cancer biology 1

Emma Bondy-Chorney1,1, Alix Denoncourt1,1, Yuka Sai1,1

  • 1Department of Cellular and Molecular Medicine and Ottawa Institute of Systems Biology, 451 Smyth Rd., Ottawa, ON KIH 8M5, Canada.

Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire
|April 20, 2018
PubMed

Insights

Lysine acetyltransferases KAT2A and KAT2B regulate nonhistone protein acetylation, impacting cancer development. This review examines their roles within the Hallmarks of Cancer framework.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cancer Biology

Background:

  • Lysine acetylation is a crucial post-translational modification affecting protein function.
  • Initially observed in histones, acetylation targets thousands of nonhistone proteins.
  • Lysine acetyltransferases (KATs) form complexes to catalyze these modifications.

Purpose of the Study:

  • To review the roles of KAT2A and KAT2B in cancer development and progression.
  • To examine KAT2A/2B-mediated acetylation within the context of the Hallmarks of Cancer.
  • To highlight specific acetylation mechanisms linked to cancer phenotypes.

Main Methods:

  • Literature review focusing on KAT2A and KAT2B.
  • Analysis of nonhistone protein acetylation in cancer.
  • Integration with the Hallmarks of Cancer framework.

Main Results:

  • KAT2A and KAT2B are implicated in various aspects of cancer biology.
  • Specific KAT2A/2B targets and their mechanisms in cancer are identified.
  • These enzymes contribute to multiple Hallmarks of Cancer.

Conclusions:

  • KAT2A and KAT2B play complex roles in cancer.
  • Understanding KAT2A/2B-mediated acetylation is vital for cancer research.
  • Systems biology approaches are essential for elucidating their functions.
Keywords:
ATACHallmarks of CancerKAT2AKAT2BSAGAacetylationacétylationcancercapacités distinctives du cancernonhistone

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