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Background: O-linked N-acyl-glycosylation may regulate protein function by competing with phosphorylation of serine residues.
Because miRNAs may regulate protein expression by translational inhibition or mRNA degradation or both mechanisms (Hausser and Zavolan, 2014; Vidigal and Ventura, 2015; Wilczynska and Bushell, 2015), these results suggest that miR-130a may decrease the MeCP2 protein level by affecting translation efficiency rather than degrading MeCP2 mRNA.
Complicating the picture still further is the data suggesting that both isoforms may regulate protein function via direct protein protein interactions (Tokuo et al., 2001; Hasegawa et al., 2006; Leiper and Vallance, 2006).
NATs are potentially functional long non-coding RNAs that may regulate protein expression via a number of possible mechanisms: transcriptional interference, chromatin remodelling, and double-stranded RNA formation leading to translational repression, RNAi or disrupting mRNA maturation and processing.
However, the functional importance of O-GlcNAc is only just emerging, with evidence to suggest that it may regulate protein activity in a manner analogous (and complementary) to phosphorylation [ 7].
In addition to ubiquitinating clients for targeting to the proteasome (6– 8), CHIP may regulate protein triage decisions by modulating the folding and degradation functions of Hsp90 via HDAC6.
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lncRNAs may regulate protein-coding (pc) gene expression at both the posttranscriptional and transcriptional level.
Although PDZ based interactions are known to be key regulators of membrane microdomain structure, stability and signaling, we have shown that this interaction may also regulate protein expression.
With the extended protein longevity, lncRNAs may then regulate protein occupancy on chromatin during cellular maintenance, as well as aid in transmission of epigenetic regulators across cell generations.
Three proteins linked to protein fate (10% of the identified proteins) may regulate the protein degradation in ARF.
We have previously shown that calcium may regulate the protein-protein interaction of ERK1/2 [56], [56], which may be mediated through the cytosolic retention sequence (CRS)/common docking motif (CD) of these ERKs.
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may extend protein
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