S100 calcium-binding protein A10 (S100A10)

S100 calcium-binding protein A10 (S100A10) is a member of the S100 family of proteins characterized by EF-hand motifs, but is uniquely Ca2+-insensitive due to mutations in its binding loops, leaving it in a constitutively active conformation[3]. It functions primarily as part of a heterotetrameric complex with annexin A2, acting as a plasminogen receptor that regulates extracellular proteolytic events, fibrinolysis, cell invasion, and angiogenesis. S100A10 is highly relevant in cancer progression, where it promotes extracellular matrix degradation and metastasis through activation of plasminogen and matrix metalloproteinases. It is also implicated in mood disorders via modulation of serotonin receptor signaling. S100A10 stability depends on annexin A2, which prevents its ubiquitin-dependent degradation. While not currently drugged clinically, it represents a potential therapeutic target in oncology and neuropsychiatric disease[1][2][3][5].

Other names

p11protein S100-A10calpactin I light chaincalpactin-1 light chainannexin II ligandANX2LGCAL1LCLP1142CGP11p10AIIt p11 subunitcellular ligand of annexin IIS100 calcium-binding protein A10 (annexin II ligand)

Inhibition of S100A10 or S100A10-annexin A2 complex would theoretically reduce plasmin generation, extracellular matrix degradation, tumor invasion, and metastasis[1][2]. Targeting S100A10 may modulate serotonin receptor trafficking/signaling in the brain, affecting antidepressant response[2].