This study reveals that YTHDF2, a reader protein for the N6-methyladenosine (m6A) modification, recruits the CCR4-NOT deadenylase complex to promote the degradation of m6A-containing RNAs. The m6A modification is abundant in eukaryotic RNAs and is reversible, playing critical roles in various biological processes. YTHDF2 binds to m6A-containing RNAs and interacts directly with the SH domain of CNOT1, a scaffolding subunit of the CCR4-NOT complex, facilitating their recruitment. This interaction is essential for the deadenylation of m6A-containing RNAs by CAF1 and CCR4. The study demonstrates that m6A-containing RNAs undergo accelerated deadenylation, which is mediated by the CCR4-NOT complex. This process is initiated by the direct interaction between YTHDF2 and CNOT1, leading to the degradation of m6A-containing RNAs. The findings highlight the role of YTHDF2 in the regulation of RNA stability through the recruitment of the CCR4-NOT complex, providing insights into the molecular mechanisms underlying m6A-mediated RNA degradation.This study reveals that YTHDF2, a reader protein for the N6-methyladenosine (m6A) modification, recruits the CCR4-NOT deadenylase complex to promote the degradation of m6A-containing RNAs. The m6A modification is abundant in eukaryotic RNAs and is reversible, playing critical roles in various biological processes. YTHDF2 binds to m6A-containing RNAs and interacts directly with the SH domain of CNOT1, a scaffolding subunit of the CCR4-NOT complex, facilitating their recruitment. This interaction is essential for the deadenylation of m6A-containing RNAs by CAF1 and CCR4. The study demonstrates that m6A-containing RNAs undergo accelerated deadenylation, which is mediated by the CCR4-NOT complex. This process is initiated by the direct interaction between YTHDF2 and CNOT1, leading to the degradation of m6A-containing RNAs. The findings highlight the role of YTHDF2 in the regulation of RNA stability through the recruitment of the CCR4-NOT complex, providing insights into the molecular mechanisms underlying m6A-mediated RNA degradation.