Intense investigation into the role of post-translational modifications, specifically phosphorylation and acetylation, has now begun, driven by the potential implications of these modifications in Alzheimer's disease (AD) and other tauopathies [ 4, 11, 16, 18, 19].
Consequently, our finding that the pattern and level of glutathiolation of nuclear proteins change during the cell cycle [24] and with the depletion of nuclear GSH could contribute to the possible implication of this modification in the control of chromatin structure dynamics (for review see [62]).
Although the biological implications of these extensive modifications remain to be elucidated, adenylation at the 3'-end has been shown to enhance the stability of mature miRNAs [38].
The nature and functional implications of these carbohydrate modifications awaits further analysis.
The functional implications of many of these modifications are yet to be determined, but these findings highlight the importance of MS in discovering novel marks that may potentially expand the basic set of the 'combinatorial histone code' and possess important regulatory roles in diseases such as cancer.
While the structural implications of this modification on these interactions is understood to some extent for p53 [ 13, 59, 60, 62, 63] little is known about p63 and p73.
Despite the generality of histone modifications as epigenetic mechanisms in eukaryotes, implication of histone modifications in fungal biology is beginning to emerge (9).
The importance of lysine acetylation is well appreciated in the context of nuclear histone modifications (Strahl and Allis, 2000), but the regulatory implications of the modification extend beyond gene regulation.
Although a clear implication of PtdIns3 P modifications has not been directly demonstrated in the aetiology of these pathologies, an important role of this lipid in cell regulation is highly suspected.
