ArticleCell reports2026
The C-terminal region of TENT5 proteins drives ER-associated mRNA polyadenylation via FNDC3 interaction.
Article in Cell reports, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Spatial regulation of mRNA polyadenylation emerges as a key mechanism shaping cellular function. The TENT5/FAM46 family comprises four non-canonical poly(A) polymerases that stabilize transcripts encoding ER-targeted proteins, with mutations linked to diseases of professional secretory cells. Using transcriptomic and proteomic profiling with systematic mutagenesis, we show how paralog-specific divergence drives distinct localization, interactions, and functions. TENT5D, the most ER-associated member, remodels the proteome, enhancing the expression of ER, ERGIC, Golgi, and lysosomal proteins. In contrast, TENT5B lacks ER targeting and regulates proteins involved in cell division. A member-specific C-terminal region that binds ER-transmembrane FNDC3 proteins is necessary and sufficient for ER localization. Mutations in this region of TENT5C, found in multiple myeloma, impair FNDC3 binding or stability, reducing immunoglobulin production and tumor-suppressive activity. Overall, we define a domain-encoded mechanism linking TENT5 localization to transcript selectivity and secretory output, with direct implications for compartmentalized mRNA regulation and development of RNA-based therapeutic strategies.
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