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 morphplogy.
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]
^Stefan C, Audhya A, Emr SD (January 2010). "Chapter 138 - FYVE Domains in Membrane Trafficking and Cell Signaling". In Bradshaw RA, Dennis EA (eds.). Handbook of Cell Signaling (Second ed.). San Diego: Academic Press. pp. 1111–1121. doi:10.1016/B978-0-12-374145-5.00138-8. ISBN978-0-12-374145-5.
