MOSPD2

Motile Sperm Domain-Containing Protein 2 (MOSPD2), also termed C19orf43 or MSPD2, is a transmembrane protein implicated in cell migration and immune regulation. Structurally characterized by a CRAL-TRIO lipid-binding domain and a MSP domain, MOSPD2 facilitates cytoskeletal remodeling through interactions with chemokine receptors, notably CXCR4. It modulates the CXCL12/CXCR4 axis, a critical pathway in leukocyte trafficking and cancer metastasis. Recent studies highlight its role in integrin-mediated adhesion and focal adhesion kinase (FAK) signaling, influencing cellular motility. MOSPD2 is functionally linked to VCP/p97 ATPase complexes, suggesting involvement in endoplasmic reticulum-associated degradation (ERAD) processes.
Dysregulation of MOSPD2 has been associated with inflammatory disorders, including multiple sclerosis and rheumatoid arthritis, due to aberrant leukocyte infiltration. In oncology, its overexpression correlates with poor prognosis in breast and pancreatic cancers. Therapeutic targeting strategies focus on monoclonal antibodies (e.g., RG6117) and small-molecule inhibitors disrupting MOSPD2-CXCR4 interactions, with preclinical models demonstrating reduced metastatic potential. A phase I trial (NCT04815811) is evaluating anti-MOSPD2 biologics for autoimmune diseases, reflecting its dual therapeutic relevance in inflammation and oncology.

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Recombinant Human Motile sperm domain-containing protein 2 (MOSPD2), partial