In addition, some non-modified serine and threonine residues could also undergo this modification (Li et al. 2003).
To date, only two T. cruzi proteins (flagellar calcium-binding protein and phosphoinositide-specific phospholipase C) have been definitively confirmed to be N-myristoylated [ 16, 37], although two studies have predicted many proteins may undergo this modification [ 46, 47].
More recently, the protein kinase IKK (IκB kinase) was shown to mediate phosphorylation of SNAP23, which in turn was shown to be important for SNARE complex formation, but the effects of an IKK inhibitor on other SNAREs were not evaluated, so it cannot be concluded that SNAP23 is the only SNARE undergoing this modification (Karim et al, 2013).
Although cellular methylation of transfected LIZ was expected to occur as such foreign, silent DNA usually undergoes this modification (as was the case Big Blue mice; You et al, 1998), we wished to guarantee methylation of λLIZ CpG sites at the outset and so pretreated λLIZ with SssI methylase before transfection.
These objectives were accomplished by successfully tyrosine phosphorylating STAM2 and Hrs (Fig. 1d), both of which undergo this post-translational modification to function in the endocytotic pathway, and by identifying changes in the interaction surfaces of Ubiquitin when bound to these post-translationally modified proteins by using STINT-NMR.
Several enzymes are known to undergo this post translational modification.
In addition, our study indicates that both aldolase and PGK1 also contain deiminated peptides, suggesting that the recognition of glycolytic enzymes by RA sera is associated with their potential to undergo this post-translational modification.
The substrate for MauG that undergoes this posttranslational modification is a precursor protein of MADH (preMADH).
Our finding that citrullination was indeed present in the myocardium extends the list of tissues known to undergo this form of post-translational modification.
It has been well-described that proteins tethered to the cell surface by means of a GPI anchor undergo this sort of post-translational modification in the ER before being sorted via the secretory pathway to their final destination, i.e., the plasma membrane.
We first engineered multiple clones of vector-matched PR-null T47D breast cancer cells expressing either WT PR-B or mutant K388R (KR) PR-B that is unable to undergo SUMO modification at Lys388; this SUMO-deficient receptor is a functional mimic for PR-B that is persistently phosphorylated on Ser294 [ 13, 41].
