S100 calcium-binding protein A16 (S100A16)

S100 calcium-binding protein A16 (S100A16) is a member of the S100 family of small, acidic, EF-hand calcium-binding proteins, characterized by its ability to bind calcium and form homodimers[1][3][6]. S100A16 is widely expressed in human tissues, including the central nervous system, adipose tissue, and bone marrow, and plays a regulatory role in diverse biological processes. It mediates cell proliferation, invasion, and migration, acts as a regulator of adipocyte differentiation, and inhibits osteogenic differentiation in mesenchymal stem cells by impacting signaling pathways such as Hippo, MAPK/JNK, and SMAD[1][5][7]. In oncology, S100A16 acts as a negative regulator of the Hippo pathway, promoting tumor progression in glioma and gastric cancer through the degradation of key tumor suppressors (e.g., LATS1 and ZO-2) via ubiquitin-mediated proteasomal degradation[1][7]. Overexpression of S100A16 correlates with worse prognosis in several cancer types, making it an emerging biomarker and a putative, yet largely unexploited, therapeutic target[1][7]. There are currently no approved drugs known to directly inhibit S100A16.

Other names

Protein S100-A16S100FAAG13DT1P1A7MGC17528Aging-associated gene 13 proteinProtein S100-Faging-associated protein 13

no specific drugs described with defined mechanisms of action against S100A16; therapeutic targeting rationale may include inhibition of protein–protein interaction or modulation of downstream signaling such as the Hippo pathway[1][7]