CLEC4E Protein, Mouse (His)

CLEC4E, a calcium-dependent lectin, functions as a pattern recognition receptor (PRR) within the innate immune system, identifying damage-associated molecular patterns (DAMPs) associated with abnormal self and pathogen-associated molecular patterns (PAMPs) from bacteria and fungi. Notably, CLEC4E recognizes mycobacterial trehalose 6,6'-dimycolate (TDM), a potent adjuvant immunomodulatory glycolipid. Interacting with the signaling adapter Fc receptor gamma chain/FCER1G, CLEC4E forms a functional complex in myeloid cells. Binding of mycobacterial TDM to this receptor complex triggers the phosphorylation of the immunoreceptor tyrosine-based activation motif (ITAM) of FCER1G, leading to the activation of SYK, CARD9, and NF-kappa-B. Consequently, this drives the maturation of antigen-presenting cells and shapes antigen-specific priming of T-cells toward the effector T-helper 1 (Th1) and T-helper 17 (Th17) cell subtypes. Additionally, CLEC4E recognizes alpha-mannose residues on pathogenic fungi, such as Malassezia, mediating macrophage activation. Acting as a monomer and homodimer, CLEC4E also interacts with SAP130 nuclear protein released from necrotic cells, promoting immune sensing of damaged self and facilitating inflammatory cell infiltration into the damaged tissue. The versatility of CLEC4E underscores its pivotal role in immune surveillance and response mechanisms.