Motile sperm domain-containing protein 2 (MOSPD2)

Motile sperm domain-containing protein 2 (MOSPD2) is an endoplasmic reticulum-resident, single-pass membrane protein that acts as a scaffold/tether to form membrane contact sites between the ER and other organelles such as endosomes, mitochondria, and Golgi[1][3][6][9]. It binds proteins bearing a FFAT motif via its MSP (Major Sperm Protein) domain and also possesses a CRAL-TRIO domain involved in recruitment to lipid droplets[8]. MOSPD2 serves key roles in cell migration: it regulates monocyte and neutrophil chemotaxis in vitro and in vivo[2][4], and is expressed on the plasma membrane of these cells. Elevated MOSPD2 levels in tumor samples, particularly breast cancer, are correlated with metastatic potential and poor prognosis. Inhibition or gene silencing of MOSPD2 reduces migration and metastasis of cancer cells and monocytes, suggesting it is a promising therapeutic target for diseases involving aberrant cell migration such as cancer and inflammation[2][4]. There are currently no approved drugs specifically targeting MOSPD2, but some experimental compounds, like BIO-VB-201, inhibit its function in preclinical research[2].

Other names

MOSPD2Motile sperm domain containing 2

Inhibitors may block chemotaxis and cell migration by interfering with MOSPD2-dependent signaling[2]