RBM33: A new regulator of N-6-methyladenosine (m6A) methylation

In this issue of Molecular Cell, Yu et al. 1 Yu F. Zhu A.C. Liu S. Gao B. Wang Y. Khudaverdyan N. Yu C. Wu Q. Jiang Y. Song J. et al. RBM33 is a unique m6A RNA binding protein that regulates ALKBH5 demethylase activity and substrate selectivity. Mol. Cell. 2023; 83: 2003-2019 Abstract Full Text Full Text PDF PubMed Scopus (3) Google Scholar identify RBM33 as a previously unrecognized m6A (N-6-methyladenosine) RNA binding protein that plays a critical role in ALKBH5-mediated m6A demethylation of a subset of mRNA transcripts by forming a complex with ALKBH5. In this issue of Molecular Cell, Yu et al. 1 Yu F. Zhu A.C. Liu S. Gao B. Wang Y. Khudaverdyan N. Yu C. Wu Q. Jiang Y. Song J. et al. RBM33 is a unique m6A RNA binding protein that regulates ALKBH5 demethylase activity and substrate selectivity. Mol. Cell. 2023; 83: 2003-2019 Abstract Full Text Full Text PDF PubMed Scopus (3) Google Scholar identify RBM33 as a previously unrecognized m6A (N-6-methyladenosine) RNA binding protein that plays a critical role in ALKBH5-mediated m6A demethylation of a subset of mRNA transcripts by forming a complex with ALKBH5. RBM33 is a unique m6A RNA-binding protein that regulates ALKBH5 demethylase activity and substrate selectivityYu et al.Molecular CellMay 30, 2023In BriefYu et al. identify RBM33 as a new m6A-binding protein that forms a complex with ALKBH5 and mediates m6A demethylation of selected transcripts by regulating ALKBH5 substrate accessibility and activity. In HNSCC cells, highly expressed RBM33 promotes HNSCC tumorigenesis by stabilizing DDIT4 in an m6A-dependent manner, thereby inducing autophagy. Full-Text PDF