HNRNPA2B1 is a nuclear reader of the m⁶A modification, acting as an adaptor that recruits the Microprocessor complex to a subset of precursor miRNAs, facilitating their processing into mature miRNAs. HNRNPA2B1 binds m⁶A-containing sites and the RGAC motif in nuclear transcripts. It mediates m⁶A-dependent primary microRNA processing events and elicits similar alternative splicing effects as the m⁶A writer METTL3. Modulation of HNRNPA2B1 and METTL3 causes similar changes to alternative splicing. HNRNPA2B1 binds to m⁶A marks in a subset of primary miRNA transcripts, interacts with the Microprocessor complex protein DGCR8, and promotes primary miRNA processing. HNRNPA2B1 loss and METTL3 depletion cause similar processing defects for these pri-miRNA precursors. HNRNPA2B1 is proposed to be a nuclear reader of the m⁶A mark and to mediate, in part, this mark's effects on primary microRNA processing and alternative splicing. HNRNPA2B1 binds to m⁶A-bearing RNAs in vivo and in vitro, and its biochemical footprint matches the m⁶A consensus motif. HNRNPA2B1 directly binds a set of nuclear transcripts and elicits similar alternative splicing effects as METTL3. HNRNPA2B1 depletion also impairs the nuclear processing of a subset of microRNAs whose maturation is dependent on METTL3 activity. HNRNPA2B1 interacts with DGCR8, a component of the pri-miRNA Microprocessor complex, and facilitates the processing of pri-miRNAs. These findings implicate HNRNPA2B1 as a nuclear reader and effector of the m⁶A mark. HNRNPA2B1 binds to m⁶A methylated RNA and interacts with the Microprocessor complex, facilitating the processing of METTL3-dependent microRNAs. HNRNPA2B1 depletion results in the accumulation of specific pri-miRNAs in the nucleus, phenocopying the effect of METTL3 depletion. HNRNPA2B1 recognizes m⁶A sequences, interacts with the Microprocessor, and facilitates the processing of a set of METTL3-dependent pri-miRNAs. These findings support a model wherein HNRNPA2B1 acts as a reader of the m⁶A mark in the nucleus and mediates, in part, the effects of m⁶A/METTL3 on microRNA processing. HNRNPA2B1 binds to m⁶A methylated RNA in vivo and in vitro, and its direct association with m⁶A methylated RNA is specific. HNRNPA2B1 interacts with theHNRNPA2B1 is a nuclear reader of the m⁶A modification, acting as an adaptor that recruits the Microprocessor complex to a subset of precursor miRNAs, facilitating their processing into mature miRNAs. HNRNPA2B1 binds m⁶A-containing sites and the RGAC motif in nuclear transcripts. It mediates m⁶A-dependent primary microRNA processing events and elicits similar alternative splicing effects as the m⁶A writer METTL3. Modulation of HNRNPA2B1 and METTL3 causes similar changes to alternative splicing. HNRNPA2B1 binds to m⁶A marks in a subset of primary miRNA transcripts, interacts with the Microprocessor complex protein DGCR8, and promotes primary miRNA processing. HNRNPA2B1 loss and METTL3 depletion cause similar processing defects for these pri-miRNA precursors. HNRNPA2B1 is proposed to be a nuclear reader of the m⁶A mark and to mediate, in part, this mark's effects on primary microRNA processing and alternative splicing. HNRNPA2B1 binds to m⁶A-bearing RNAs in vivo and in vitro, and its biochemical footprint matches the m⁶A consensus motif. HNRNPA2B1 directly binds a set of nuclear transcripts and elicits similar alternative splicing effects as METTL3. HNRNPA2B1 depletion also impairs the nuclear processing of a subset of microRNAs whose maturation is dependent on METTL3 activity. HNRNPA2B1 interacts with DGCR8, a component of the pri-miRNA Microprocessor complex, and facilitates the processing of pri-miRNAs. These findings implicate HNRNPA2B1 as a nuclear reader and effector of the m⁶A mark. HNRNPA2B1 binds to m⁶A methylated RNA and interacts with the Microprocessor complex, facilitating the processing of METTL3-dependent microRNAs. HNRNPA2B1 depletion results in the accumulation of specific pri-miRNAs in the nucleus, phenocopying the effect of METTL3 depletion. HNRNPA2B1 recognizes m⁶A sequences, interacts with the Microprocessor, and facilitates the processing of a set of METTL3-dependent pri-miRNAs. These findings support a model wherein HNRNPA2B1 acts as a reader of the m⁶A mark in the nucleus and mediates, in part, the effects of m⁶A/METTL3 on microRNA processing. HNRNPA2B1 binds to m⁶A methylated RNA in vivo and in vitro, and its direct association with m⁶A methylated RNA is specific. HNRNPA2B1 interacts with the