C-type lectin domain family 1 member B (CLEC1B)

C-type lectin domain family 1 member B (CLEC1B), also known as CLEC-2, is a type II transmembrane C-type lectin-like receptor expressed predominantly on platelets and certain myeloid and NK cells. CLEC1B functions as a receptor for the lymphatic endothelial cell marker podoplanin, playing a crucial role in platelet activation, vascular integrity, and immune cell signaling. Upon binding to its ligands—including podoplanin or the snake venom protein rhodocytin—CLEC1B initiates a signaling cascade involving SRC and SYK tyrosine kinases and PLCG2, promoting platelet aggregation and contributing to hemostasis as well as immune responses. CLEC1B can also act as an attachment factor for human immunodeficiency virus type 1 (HIV-1), facilitating viral capture by platelets. Disorders associated with CLEC1B function include bleeding diatheses due to altered platelet activation, and it is implicated in cancer biology and infection[2][3].

Other names

CLEC-2C-type lectin-like receptor 2CLL-2platelet receptor for podoplaninC-type lectin-like receptor B

Ligand binding (e.g., to podoplanin or rhodocytin from snake venom) induces CLEC1B clustering and signaling via SRC and SYK tyrosine kinases, subsequently activating downstream pathways such as PLCG2[3].