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A more recent version of this article appeared on February 1, 2003
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Submitted on April 11, 2002
Revised on July 23, 2002
Accepted on October 25, 2002
1 Laboratory of Cell Biology, NHLBI, National Institutes of Health, Bethesda, MD 20892
* Corresponding author. E-mail address: jdonalds{at}helix.nih.gov.
The trafficking of two plasma membrane (PM) proteins that lack clathrin internalization sequences, major histocompatibility complex class I (MHCI) and interleukin 2 receptor 
subunit (Tac), was compared to that of PM proteins internalized via clathrin. MHCI and Tac were internalized into endosomes that were distinct from those containing clathrin cargo. At later times, a fraction of these internalized membranes were observed in Arf6-associated, tubular reycling endosomes whereas another fraction acquired early endosomal autoantigen 1 (EEA1) prior to fusion with the "classical" early endosomes containing the clathrin-dependent cargo, LDL. After convergence, cargo molecules from both pathways eventually arrived, in a Rab7-dependent fashion, at late endosomes and were degraded. Expression of a constitutively active mutant of Arf6, Q67L, caused MHCI and Tac to accumulate in enlarged PIP2-enriched vacuoles, devoid of EEA1 and inhibited their fusion with clathrin cargo-containing endosomes and hence blocked degradation. By contrast, trafficking and degradation of clathrin-cargo was not affected. A similar block in transport of MHCI and Tac was reversibly induced by a PI3-kinase inhibitor, implying that inactivation of Arf6 and acquisition of PI3P are required for convergence of endosomes arising from these two pathways.
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