Transmembrane 7 superfamily member 3 (TM7SF3)

Transmembrane 7 superfamily member 3 (TM7SF3) is a seven-transmembrane protein regulated by p53 and plays a key role in maintaining cellular homeostasis. Uniquely, TM7SF3 localizes to nuclear speckles, where it forms complexes with pre-mRNA splicing factors and regulates alternative splicing, especially at the 3' end of introns, affecting over 300 genes. In pancreatic β-cells, TM7SF3 supports cell survival and normal insulin secretion by attenuating endoplasmic reticulum stress and the unfolded protein response. In the liver, TM7SF3 limits fibrosis by controlling splicing of the transcription factor TEAD1 in hepatic stellate cells, affecting cell activation and proliferation. TM7SF3 acts as a homeostatic factor across several stress models and is itself transcriptionally regulated by p53, serving as a feedback attenuator of cellular stress responses. To date, no clinically approved drugs directly target TM7SF3, but its unique nuclear-localized regulatory functions make it notable among seven-transmembrane proteins[1][2][3][4][5][6][7].

Other names

Seven span transmembrane proteinSeven transmembrane protein TM7SF3

Not directly druggable/mechanistically targeted by approved drugs; research explores modulation of alternative splicing and cellular stress through genetic or antisense approaches