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Tuftelin 1 (TUFT1) is an acidic, phosphorylated glycoprotein best known for its role in the mineralization and structural organization of dental enamel, as well as a broader role in structuring the epidermis[1][3][4][5]. Originally identified in developing tooth enamel, tuftelin belongs to the group of enamel matrix proteins known as nonamelogenins. It is transiently expressed during amelogenesis and may act as an initiator of enamel mineralization; mutations in or altered expression of TUFT1 are implicated in disordered enamel development, including amelogenesis imperfecta and increased susceptibility to dental caries[1][3][5]. Beyond dental tissues, TUFT1 is also found in other tissues and has been increasingly linked to cell proliferation, migration, EMT, and cancer progression, particularly via the PI3K/AKT pathway in renal cell carcinoma and hepatocellular carcinoma[2]. TUFT1 is therefore regarded as both a tissue structural protein and a potential oncogenic effector; high TUFT1 expression can serve as a prognostic biomarker for poor clinical outcomes in certain cancers[2]. While not a classical receptor, enzyme, or transporter, TUFT1 may represent an emerging therapeutic target in oncology and remains an important protein in dental and epithelial biology[2][5].
Not directly targeted by any approved drugs. In cancer contexts, effects mediated through the PI3K/AKT pathway (renal cell carcinoma, hepatocellular carcinoma), mTORC1 signaling pathway (lung cancer), or Rab5/Rac1 pathway (breast cancer)
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