EEA1 localizes exclusively to early endosomes?and has an important role in endosomal trafficking. EEA1 binds directly to the phospholipid phosphatidylinositol 3-phosphate?through its C-terminalFYVE domain?and forms a homodimer?through a?coiled coil. EEA1 acts as a tethering molecule that couples vesicle docking with SNAREs such as?N-ethylmaleimide sensitive fusion protein, bringing the endosomes physically closer and ultimately resulting in the fusion and delivery of endosomal cargo. Due to the proteins importance in vesicular trafficking, a number of intracellular bacteria prevent EEA1 recruitment to the vacuole.Mycobacterium tuberculosis?is known to inhibit the recruitment of EEA1 to the phagosomal membrane through CamKII. Legionella pneumophila?also prevents EEA1 recruitment through a currently unknown mechanism.[5] Interestingly, the related pathogen Legionella longbeachae?recruits EEA1 and appears to replicate within a modified early endosome.
