Article abstract
Nature Cell Biology 10, 30 - 41 (2008)
Published online: 16 December 2007 | doi:10.1038/ncb1666
ARF1 is directly involved in dynamin-independent endocytosis
Sudha Kumari1 & Satyajit Mayor1
Abstract
Endocytosis of glycosylphosphatidyl inositol (GPI)-anchored proteins (GPI-APs) and the fluid phase takes place primarily through a dynamin- and clathrin-independent, Cdc42-regulated pinocytic mechanism. This mechanism is mediated by primary carriers called clathrin-independent carriers (CLICs), which fuse to form tubular early endocytic compartments called GPI-AP enriched endosomal compartments (GEECs). Here, we show that reduction in activity or levels of ARF1 specifically inhibits GPI-AP and fluid-phase endocytosis without affecting other clathrin-dependent or independent endocytic pathways. ARF1 is activated at distinct sites on the plasma membrane, and by the recruitment of RhoGAP domain-containing protein, ARHGAP10, to the plasma membrane, modulates cell-surface Cdc42 dynamics. This results in the coupling of ARF1 and Cdc42 activity to regulate endocytosis at the plasma membrane. These findings provide a molecular basis for a crosstalk of endocytosis with secretion by the sharing of a key regulator of secretory traffic, ARF1.
- National Centre for Biological Science (TIFR), Bellary Road, Bangalore 560 065, India.
Correspondence to: Satyajit Mayor1 e-mail: mayor@ncbs.res.in
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