YTHDC1 is a nuclear m6A reader protein that plays crucial roles in RNA metabolism and cellular homeostasis. Its primary function involves recognizing and binding N6-methyladenosine (m6A)-modified RNAs to regulate alternative splicing 1. YTHDC1 promotes exon inclusion by recruiting splicing factor SRSF3 while blocking SRSF10 binding, with transcriptome analysis revealing that YTHDC1-regulated splicing patterns mirror SRSF3 but oppose SRSF10 1. The protein undergoes liquid-liquid phase separation in an m6A-dependent manner, forming nuclear YTHDC1-m6A condensates (nYACs) that protect m6A-modified mRNAs from degradation by the PAXT complex and exosome 2. In cancer contexts, YTHDC1 functions as a tumor suppressor by modulating ferroptosis resistance through regulation of FSP1 mRNA stability via alternative polyadenylation 3. YTHDC1 also maintains autophagy by stabilizing SQSTM1 mRNA in cooperation with ELAVL1/HuR 4. Recent studies reveal that YTHDC1 can be post-translationally modified by lactylation at K82, which enhances its phase separation and promotes stability of oncogenic transcripts like BCL2 and E2F2 5. The increased number of nYACs in acute myeloid leukemia cells compared to normal hematopoietic cells suggests YTHDC1's importance in maintaining leukemic cell survival and undifferentiated states 2.