{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nSYNCRIP, also known as hnRNP Q or NSAP1, is a versatile RNA‐binding protein central to multiple aspects of RNA metabolism. It modulates pre‐mRNA splicing—as demonstrated by its differential control of exon 7 inclusion in SMN2 transcripts—and associates with mRNA granules that are actively transported in neuronal dendrites, contributing to local mRNA stabilization and translation."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn viral contexts, SYNCRIP enhances internal ribosome entry site (IRES)–dependent translation and is required for efficient replication of Hepatitis C virus RNA. Moreover, it directly interacts with the HIV-1 Rev protein—together with additional hnRNP family members—to influence viral gene expression and RNA export, underscoring its importance in the life cycles of diverse viruses."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "3", "end_ref": "6"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nThe activity of SYNCRIP is further regulated by post‐translational modifications and specific structural features. It is a substrate for arginine methylation by PRMT1, and its phosphorylation state is modulated by dephosphorylation via SHP2. In addition, its unique N-terminal acidic domain exhibits a defined globular structure with the capacity to bind ATP, suggesting that both chemical modifications and ligand interactions fine-tune SYNCRIP’s function."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "7", "end_ref": "10"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn oncogenic settings, SYNCRIP supports the translation of key regulators that drive cell proliferation and tumor progression. It promotes the synthesis of proteins such as Aurora-A kinase and sustains leukemia stem cell programs through maintenance of HOXA9 levels. Additionally, stabilization of SYNCRIP by galectin-3 and its modulation by oncogenic long noncoding RNAs observed in pancreatic cancer further implicate this RBP as a contributor to tumorigenesis and as a potential therapeutic target—findings that are underlined further by its co-deletion in certain subtypes of T-cell acute lymphoblastic leukemia."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "11", "end_ref": "16"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nSYNCRIP also exerts control over miRNA biogenesis and mRNA translation. It facilitates the processing of the primary let-7a transcript and directs the sorting of a specific group of miRNAs into exosomes via a conserved N-terminal RNA recognition unit (NURR). Additionally, it can inhibit the translation of certain target mRNAs such as YB-1 by displacing positive regulators like the poly(A)-binding protein from critical regulatory elements."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "17", "end_ref": "19"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond these functions, SYNCRIP interacts with components of the RNA-editing machinery. Its N-terminal acidic domain mediates an interaction with APOBEC1—an enzyme involved in RNA editing events—and facilitates the binding of APOBEC1 to specific mRNAs such as IL8, thereby enhancing their stability and production. Structural analyses further delineate how this acidic region supports these interactions."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "20", "end_ref": "22"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nSYNCRIP is also implicated in neurodegenerative and autophagic pathways. It is frequently found in pathological neuronal inclusions associated with frontotemporal lobar degeneration with FUS pathology, and it has been shown to play a crucial role in stimulating early events in autophagosome biogenesis—findings that suggest misregulation of SYNCRIP may contribute to diseases such as oculopharyngeal muscular dystrophy."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "23"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Hiroko Bannai, Kazumi Fukatsu, Akihiro Mizutani, et al. 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