EEA1
Protein-coding gene in humans
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The gene EEA1 encodes for the 1400 amino acid protein, Early Endosome Antigen 1.
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| Aliases | EEA1, MST105, MSTP105, ZFYVE2, early endosome antigen 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 605070; MGI: 2442192; HomoloGene: 37822; GeneCards: EEA1; OMA:EEA1 - orthologs | ||||||||||||||||||||||||||||||||||||||||||||||||||
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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-terminal FYVE 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.
Function
EEA1 is a RAB5A effector protein which binds via an N-terminal zinc finger domain and is required for fusion of early and late endosomes and for sorting at the early endosome level.[5][6]
EEA1 plays a role in endocytosis and is recruited by Rab5-GTP to endosomal membranes.[7] EEA1 may be regulated through monoubiquination, affecting endosome fusion and trafficking.[8] Ubiquitin selective segregase p97 may regulate EEA1's tethering ability, affecting its endosome trafficking and morphology.
Involvement in pathogenesis
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.[9] Legionella pneumophila also prevents EEA1 recruitment through a currently unknown mechanism.[10] The related pathogen Legionella longbeachae recruits EEA1 and appears to replicate within a modified early endosome.[11]