VSTM1

VSTM1, also referred to as SIRL1, is a transmembrane protein characterized by a V-type domain. VSTM1 serves as an immune checkpoint receptor mainly found on myeloid cells, including neutrophils and monocytes/macrophages. VSTM1 regulates by transmitting inhibitory signals through its immune receptor tyrosine-based inhibitory motifs (ITIMs). Upon ligand binding, VSTM1 recruits tyrosine phosphatases SHP1 and SHP2, which possess Src homology domains, to suppress immune cell activation. This inhibition affects processes such as the reduction of reactive oxygen species production induced by Fc receptors and the enhancement of the respiratory burst. By modulating the activation state of immune cells, VSTM1 is crucial for the equilibrium between immune tolerance and response. In the context of systemic lupus erythematosus (SLE), VSTM1's role is highlighted by the inability of oxidized galectin-1 to bind to it, resulting in elevated neutrophil reactive oxygen species (ROS) levels and contributing to SLE pathogenesis. Given these functions, VSTM1 is emerging as a potential therapeutic target for autoimmune disease treatment.

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Recombinant Human V-set and transmembrane domain-containing protein 1 (VSTM1), partial