
IndraLab
Statements
sparser
"It possesses several RNA-binding structural domains, namely four C-terminal heterologous ribonucleoprotein K homology (KH) (KH1-KH4) domains and two N-terminal RNA recognition motifs [ xref ], and are involved in the regulation of a wide range of RNA processing mechanisms, such as localization, stability, and translation [ xref ]."
sparser
"It contains three K-homology domains (KH1-KH3) responsible for nucleic acid binding, one K protein interactive domain (KI) responsible for protein binding, and a nuclear-cytoplasmic shuttling domain (KNS) that confers the ability to translocate bidirectionally through the nuclear pore complex."
| PMC
sparser
"It is well known that post‐transcriptional modifications of messenger RNAs (mRNAs), among which m 6 A is the most abundant internal RNA modification, regulate genes expression by influencing mRNA splicing, stability, translocation and translation. [ xref ] m 6 A modification is deposited by “writers” the methyltransferase complex containing the methyltransferase‐like 3 and 14 proteins (METTL3 and METTL14) and their regulator Wilms tumor 1‐associated protein, and removed by “erasers” demethylases: fat mass and obesity‐associated protein (FTO) and α‐ketoglutarate dependent dioxygenase AlkB homolog 5 (ALKBH5). [ xref , xref , xref , xref ] Moreover, m 6 A modification exerts its biological functions by “readers”: YTH (YT521‐B homology) domain proteins including YTHDC1–2 and the YTH‐family proteins YTHDF1–3 as well as insulin‐like growth factor 2 mRNA binding proteins IGF2BP1–3. [ xref ] Among these m 6 A readers, IGF2BP2 binds RNA via its six characteristic RNA‐binding domains, containing two RNA recognition motifs (RRM1 and RRM2) and four K Homology (KH) domains (KH1–KH4). [ xref ] Dysregulation of IGF2BP2 is implicated in certain diseases such as diabetes and cancer, nevertheless, little is known about IGF2BP2's functions in immunity."