Claudin-25 (CLDN25)

Claudin-25 is a non-classic member of the claudin family, which are four-transmembrane domain proteins fundamental to the structure and function of tight junctions in mammalian epithelial and endothelial cells[1][2]. Claudins control paracellular transport, maintaining cell polarity and contributing to tissue barrier function by regulating passage of ions and solutes between cells[2][3]. Claudin-25 is encoded by the CLDN25 gene (HGNC: 37218) and has an atypical structure compared to other claudins, with less conserved amino acid sequences and some unique motifs[1]. It lacks several features critical for canonical tight junction assembly, such as the ZO-1 binding motif and cis-polymerization elements found in other claudins[1]. Unlike more established claudins, CLDN25 is not well-studied, and its specific physiological roles and relevance to disease are largely unknown[1]. A recent report linked a CLDN25 gene mutation to an atypical leukodystrophy, suggesting disease relevance in rare contexts, but the underlying function remains enigmatic and may differ across cell types[1]. As of now, there are no reported drugs targeting this protein, nor is it established as a validated therapeutic target or common biomarker[1][2].

Other names

Claudin-25CLDN25claudin-25putative claudin-25Claudin containing domain 1