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Significance IRBIT (inositol 1,4,5-trisphosphate receptor binding protein released with inositol 1,4,5-trisphosphate) contributes to calcium signaling, electrolyte transport, mRNA processing, genomic integrity, and catecholamine homeostasis through its interaction with multiple targets. However, how IRBIT selectively binds and regulates appropriate target molecules in a certain condition is poorly understood. In this study, we found that N-terminal variation of Long-IRBIT by splicing affected protein stability and target selectivity. In addition, IRBIT and Long-IRBIT splice variants formed homo- and heteromultimers. N-terminal variation of IRBIT family members mediates the regulation of multiple signaling pathways.

Splicing variation of Long-IRBIT determines the target selectivity of IRBIT family proteins