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2016 ; 11
(3
): 547-53
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Regulation of Methyllysine Readers through Phosphorylation
#MMPMID26726824
ACS Chem Biol
2016[Mar]; 11
(3
): 547-53
PMID26726824
show ga
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.