Triggering receptor expressed on myeloid cells-like protein 1 (TREML1)

Triggering receptor expressed on myeloid cells-like protein 1 (TREML1) is a type I transmembrane receptor and member of the immunoglobulin superfamily, principally expressed on platelets and megakaryocytes[1][2][6]. Its structure is characterized by a single extracellular immunoglobulin-like V-set domain and a cytoplasmic tail containing immunoreceptor tyrosine-based inhibitory motifs (ITIMs), which confer the ability to modulate intracellular signaling[1][2]. TREML1 is stored in platelet α-granules and rapidly translocated to the platelet surface upon activation, where it facilitates platelet aggregation by binding fibrinogen and modulates inflammatory and immune responses[1][2]. Additionally, a soluble form (sTLT-1) is released during platelet activation, with roles in both thrombosis and inflammation. TREML1 is genetically and functionally distinct from activating TREM family members such as TREM1 and TREM2, though it is found within the same chromosomal cluster[1][4]. Variants or altered expression of TREML1 are linked to a variety of pathological processes, including bleeding disorders, sepsis, vascular inflammation, and certain immune-mediated conditions[1][2]. There are currently no clinically approved drugs directly targeting TREML1, but its roles make it a possible future therapeutic and diagnostic target.

Other names

TREML1Trem-like transcript 1 proteinTLT-1TLT1dJ238O23.3GLTL1825PRO3438Triggering receptor expressed on myeloid cells-like protein 1

Modulation of platelet aggregation by binding to fibrinogen and regulating thrombin-mediated signaling; Release of soluble TLT-1, which may modulate inflammation and coagulation pathways; Interaction with signaling adaptors such as SHP-1 and SHP-2 via immunoreceptor tyrosine-based inhibition motif (ITIM)