BEX1 Human

BEX1 is an intrinsically disordered protein (IDP), meaning it lacks a fixed or stable three-dimensional structure under physiological conditions. This property allows BEX1 to interact with multiple partners and participate in various cellular processes . BEX1 shows cell density-dependent accumulation as a condensate either in nucleoli at a low cell density or at the apical cell surface at a high cell density .

BEX1 is involved in the regulation of transcription by RNA polymerase II. It enables RNA polymerase II-specific DNA-binding transcription factor binding activity and is part of the transcription regulator complex . Additionally, BEX1 plays a role in cell cycle progression and neuronal differentiation by inhibiting neuronal differentiation in response to nerve growth factor (NGF) .

BEX1 has been implicated in various diseases, including viral myocarditis and certain cancers. For instance, BEX1 has been identified as a novel stress-regulated pro-inflammatory factor in the heart, playing a cardioprotective role during viral infections . In the context of coxsackievirus B3 (CVB3)-induced cardiomyopathy, BEX1 limits viral replication in cardiomyocytes and regulates interferon beta (IFN-β) expression in infected cells .

Research on BEX1 has revealed its potential as an antiviral agent. Studies have shown that BEX1 is necessary and sufficient to counteract viral replication in both isolated primary cardiomyocytes and mouse embryonic fibroblasts, suggesting a broader applicability of BEX1 as an antiviral agent beyond CVB3, including Influenza A and Sendai virus .

In addition to its role in viral infections, BEX1 is also involved in the regulation of the cell cycle and neuronal differentiation. It acts as a link between the cell cycle and neurotrophic factor signaling, possibly by functioning as an upstream modulator of receptor signaling, coordinating biological responses to external signals with internal cellular states .