Journal
ACS CHEMICAL BIOLOGY
Volume 11, Issue 3, Pages 547-553Publisher
AMER CHEMICAL SOC
DOI: 10.1021/acschembio.5b00802
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Funding
- National Institutes of Health [R01 GM106416, GM100907, R01 GM110058, T32AA007464]
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Methyllysine post-translational modifications (PTMs) of histones create binding sites for evolutionarily conserved reader domains that link nuclear host proteins and chromatin-modifying complexes to specific genomic regions. In the context of these events, adjacent histone PTMs are capable of altering the binding activity of readers toward their target marks. This provides a mechanism of combinatorial readout of PTMs that can enhance, decrease, or eliminate the association of readers with chromatin. In this Perspective, we focus on recent studies describing the impact of dynamic phospho-serine/threonine/ tyrosine marks on the interaction of methyllysine readers with histones, summarize mechanistic aspects of the phospho/methyl readout, and highlight the significance of crosstalk between these PTMs. We also demonstrate that in addition to inhibiting binding and serving as a true switch, promoting dissociation of the methyllysine readers from chromatin, the phospho/methyl combination can act together in a cooperative manner thus adding a new layer of regulatory information that can be encoded in these dual histone PTMs.
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