Cesaro E, De Cegli R, Medugno L, Florio F, Grosso M, Lupo A et al. The Kruppel-like zinc finger protein ZNF224 recruits the arginine methyltransferase PRMT5 on the transcriptional repressor complex of the aldolase A gene. J Biol Chem 2009; 284: 32321-32330....
Hepatitis B X-interacting protein (HBXIP). Epidermal growth factor receptor (EGFR). Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1). P-element-induced wimpy testis (PIWI)-interacting RNAs (piRNAs). YTH N6-methyladenosine RNA binding protein F1 (YTHDF1) Full size image Collectively...
Protein-lysine methylation is a common posttranslational modification (PTM) throughout the human proteome that plays important roles in diverse biological processes. In humans, there are >100 known and candidate protein lysine methyltransferases (PKMTs), many of which are linked to human diseases. ...
The A. suum PEAMT1-like-protein (depicted in FIG. 1 as SEQ ID NO 7) is approximately 52% identical (in the region of shared homology) to the C. elegans PEAMT1-like proteins (depicted in FIG. 7 as SEQ ID NO: 19 and 20). The similarity between the PEAMT1 proteins from A. ...
Knockdown of ATG5, ATG7, ULK1 and BECN1 at the mRNA (A) and protein level (B) using specific siRNAs. Glioma cells were transfected with ATG- targeting siRNA for 48 h, followed by 2 μM BIX01294 for 24 h. (A) Each bar represents the mean ± SEM of three ...
[24]. Additionally, the METTL3 interacts with poly(A)-binding protein cytoplasmic 1 (PABPC1) to stabilize the RNA loop structure by promoting PABPC1 and eukaryotic translation initiation factor 4E (eIF4F) binding, thereby preferentially promoting RNA translation of epigenetic factors without m6A ...
In breast cancer, PRMT5 is a key regulator of BCSC proliferation, self-renewal [24], and genome stability [25]. PRMT5 requires its partner methylome protein (MEP50/WDR77) to form an active enzymatic complex [26]. CDK4 phosphorylates MEP50 and increases PRMT5/MEP50 activity, resulting in...
As a nonstructural polyprotein, HEV ORF1 contains one or several functional domains able to modulate the IFN-I system. The macrodomain, the PCP domain and the Met domain have been described as antagonists of the signalling cascade leading to IFN synthesis [35,36]. However, nothing is known ...