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Vol. 11, Issue 8, 2657-2671, August 2000
and
*Department of Cell Biology and Anatomy, University of Arizona,
Tucson, Arizona; EEA1 is an early endosomal Rab5 effector protein that has been
implicated in the docking of incoming endocytic vesicles before fusion
with early endosomes. Because of the presence of complex endosomal
pathways in polarized and nonpolarized cells, we have examined the
distribution of EEA1 in diverse cell types. Ultrastructural analysis
demonstrates that EEA1 is present on a subdomain of the early sorting
endosome but not on clathrin-coated vesicles, consistent with a role in
providing directionality to early endosomal fusion. Furthermore, EEA1
is associated with filamentous material that extends from the
cytoplasmic surface of the endosomal domain, which is also consistent
with a tethering/docking role for EEA1. In polarized cells (Madin-Darby
canine kidney cells and hippocampal neurons), EEA1 is present on a
subset of "basolateral-type" endosomal compartments, suggesting
that EEA1 regulates specific endocytic pathways. In both epithelial
cells and fibroblastic cells, EEA1 and a transfected apical endosomal
marker, endotubin, label distinct endosomal populations. Hence, there
are at least two distinct sets of early endosomes in polarized and
nonpolarized mammalian cells. EEA1 could provide specificity and
directionality to fusion events occurring in a subset of these
endosomes in polarized and nonpolarized cells.
European Molecular Biology Laboratory,
Heidelberg, Germany; §Centre for Microscopy and
Microanalysis, Department of Physiology and Pharmacology, and Centre
for Molecular and Cellular Biology, University of Queensland, Brisbane,
Australia; and Department of Pathology and Immunology,
Monash University, Melbourne, Australia
Present address: Hoechst Marion Roussel,
Core Research Functions, D-65926 Frankfurt am Main, Germany.
¶
Corresponding author. E-mail address:
r.parton{at}mailbox.uq.edu.au.
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