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The magnitude of changes in phosphorylation levels between the dormant and germinating spore phosphoproteomes, reinforces the view that phospho-modifications could play a key role in rapidly modulating protein activity throughout this cellular conversion.
It is conceivable that the increase in asMYO5A levels in prostate cells in response to androgen affects the relative levels of the alternatively spliced forms of MYO5A, thus modulating protein activity or specificity.
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Flux in nutrients thereby modulates protein activity by flux in O-linked glycosylation of proteins.
Protein phosphorylation often leads to structural changes in proteins, and such changes can directly modulate protein activity and reflect changes in interaction partners or subcellular localization [ 14].
Quantitative comparison of dormant and germinating spore phosphoproteomes revealed phosphorylation dynamics, indicating that phospho-modifications could modulate protein activity during this cellular transition.
S-sulfhydration (herein used to differentiate between a mechanism of sulfur transfer for the biogenesis of sulfur-containing cofactors and a redox regulated posttranslational modification) is now recognized as a mechanism by which H2S can modulate protein activity.
The high copy numbers of Yfr1 raise the question of whether this RNA acts as a trans-encoded sRNA through base pairing with its targets, or whether it modulates protein activity.
miRNAs can modulate protein activities by altering mRNA stability, translational efficiency or localization [ 53, 54].
Other ncRNAs can bind to proteins in order to modulate protein activity [ 9].
However, like coenzymes that modulate protein activity, it is possible that lncRNAs may affect protein function more directly.
It has been shown that sRNAs affect mRNA degradation and translation and modulate protein activity [ 14, 16].
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