SUMO modification (sumoylation) is a newly discovered form of post-translational modification, which modulates protein function through covalent attachment to lysine residues within targeted proteins.
However, posttranslational modifications seem more important which modulate the hnRNPs activities during biological processes.
Glycosylation is an abundant eukaryotic protein modification reaction, which modulates a variety of cellular processes, including protein folding, trafficking, cell cell interactions, cell signaling, and the host immune response.
Many E3 ligases and some DUBs undergo post-translational modifications, such as ubiquitination or sumoylation, which modulate the recognition of their substrates [25].
It is recognized that histone modification is catalyzed by several enzymes which modulate the histone markers.
In response to these signals, p53 undergoes a variety of post-translational modifications, such as phosphorylation, acetylation and sumolation, which modulate its stability and activity [ 5].
HDACs undergo various posttranslational modifications, such as phosphorylation, sumoylation, ubiquitination, S-nitrosylation and acetylation, which modulate enzymatic activity, protein stability and their interactions with other proteins.
The N-terminal tails of histones are decorated in covalent posttranslational modifications which can modulate the accessibility of the underlying DNA for diverse chromatin transactions such as transcriptional control, chromosome segregation, and the repair of DNA damage.
Kornblihtt indicates that diverse splicing factors associate with a carboxy terminal domain (CTD) of RNAPII [ 47], whereas phosphorylated CTD of RNAPII can recruit Histone-lysine N-methyltransferase SETD2, which modulates the histone modification H3K36me3 [ 48].
We hypothesize that CDR internalization affects activity-dependent modifications of synaptic integrity, stability, and function of target proteins, which modulates the synaptic Ca2+ transient by mediating over-activation of calpain-2 [ 5, 17].
