RNA-binding proteins (RBPs) play a critical role in microRNA (miRNA) biogenesis, influencing various steps including processing, nuclear export, cytosolic processing, and RISC formation. miRNAs are small non-coding RNAs that regulate gene expression by binding to complementary sequences in the 3' untranslated regions (UTR) of target mRNAs. The biogenesis of miRNAs involves a series of steps, starting with the transcription of miRNA genes by RNA polymerase II, followed by processing by Drosha and Dicer to generate mature miRNAs. RBPs are essential for the recognition and processing of miRNA precursors, as well as for the regulation of miRNA function. They interact with various components of the miRNA pathway, including the microprocessor complex, which is responsible for the initial processing of pri-miRNAs. RBPs such as SRSF3, KSRP, hnRNPA1, TDP-43, and LIN28B are involved in the processing of pri-miRNAs, either promoting or inhibiting the cleavage by Drosha. Additionally, RBPs such as ADAR1, DAZL, and YB-1 are involved in the processing of pre-miRNAs by Dicer. RBPs also play a role in the nuclear export of pre-miRNAs, with Exportin 5 and Exportin 1 being involved in this process. Furthermore, RBPs are involved in the formation of RISC, the functional complex that carries out miRNA-mediated gene silencing. RBPs such as CSDE1 and FMRP interact with AGO proteins and miRNAs to regulate their function. Non-canonical miRNA biogenesis pathways, such as mirtron biogenesis and miRNA processing from snoRNAs and tRNAs, also involve RBPs. These pathways bypass the canonical processing steps and utilize alternative mechanisms for cleavage, export, and RISC loading. The cluster assistance phenomenon, where sub-optimal pri-miRNAs are processed more efficiently due to the presence of optimal pri-miRNAs in the same transcript, also involves RBPs such as SAFB2 and ERH. Overall, RBPs are essential for the regulation of miRNA biogenesis and function, and their involvement in various steps of the miRNA pathway is a key area of research.RNA-binding proteins (RBPs) play a critical role in microRNA (miRNA) biogenesis, influencing various steps including processing, nuclear export, cytosolic processing, and RISC formation. miRNAs are small non-coding RNAs that regulate gene expression by binding to complementary sequences in the 3' untranslated regions (UTR) of target mRNAs. The biogenesis of miRNAs involves a series of steps, starting with the transcription of miRNA genes by RNA polymerase II, followed by processing by Drosha and Dicer to generate mature miRNAs. RBPs are essential for the recognition and processing of miRNA precursors, as well as for the regulation of miRNA function. They interact with various components of the miRNA pathway, including the microprocessor complex, which is responsible for the initial processing of pri-miRNAs. RBPs such as SRSF3, KSRP, hnRNPA1, TDP-43, and LIN28B are involved in the processing of pri-miRNAs, either promoting or inhibiting the cleavage by Drosha. Additionally, RBPs such as ADAR1, DAZL, and YB-1 are involved in the processing of pre-miRNAs by Dicer. RBPs also play a role in the nuclear export of pre-miRNAs, with Exportin 5 and Exportin 1 being involved in this process. Furthermore, RBPs are involved in the formation of RISC, the functional complex that carries out miRNA-mediated gene silencing. RBPs such as CSDE1 and FMRP interact with AGO proteins and miRNAs to regulate their function. Non-canonical miRNA biogenesis pathways, such as mirtron biogenesis and miRNA processing from snoRNAs and tRNAs, also involve RBPs. These pathways bypass the canonical processing steps and utilize alternative mechanisms for cleavage, export, and RISC loading. The cluster assistance phenomenon, where sub-optimal pri-miRNAs are processed more efficiently due to the presence of optimal pri-miRNAs in the same transcript, also involves RBPs such as SAFB2 and ERH. Overall, RBPs are essential for the regulation of miRNA biogenesis and function, and their involvement in various steps of the miRNA pathway is a key area of research.