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Here we show that cytochalasin D (CD) treatment inhibited formation of the AlF-induced protrusions and shifted the distribution of ARF6 to a tubular membrane compartment emanating from the juxtanuclear region of cells, which resembled the compartment where the GTP-binding defective mutant of ARF6 localized. This membrane compartment was distinct from transferrin-positive endosomes, could be detected in the absence of ARF6 overexpression or CD treatment, and was accessible to loading by PM proteins lacking clathrin\/AP-2 cytoplasmic targeting sequences, such as the IL-2 receptor \u03b1 subunit Tac. ARF6 and surface Tac moved into this compartment and back out to the PM in the absence of pharmacologic treatment. Whereas AlF treatment blocked internalization, CD treatment blocked the recycling of wild-type ARF6 and Tac back to the PM; these blocks were mimicked by expression of ARF6 mutants Q67L and T27N, which were predicted to be in either the GTP- or GDP-bound state, respectively. Thus, the ARF6 GTP cycle regulates this membrane traffic pathway. The delivery of ARF6 and membrane to defined sites along the PM may provide components necessary for remodeling the cell surface and the underlying actin cytoskeleton.<\/jats:p>","DOI":"10.1083\/jcb.139.1.49","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T16:47:50Z","timestamp":1027702070000},"page":"49-61","update-policy":"https:\/\/doi.org\/10.1083\/jcb.crossmarkpolicy","source":"Crossref","is-referenced-by-count":424,"title":["ADP-Ribosylation Factor 6 Regulates a Novel Plasma Membrane Recycling Pathway"],"prefix":"10.1083","volume":"139","author":[{"given":"Harish","family":"Radhakrishna","sequence":"first","affiliation":[{"name":"Laboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892"}]},{"given":"Julie G.","family":"Donaldson","sequence":"additional","affiliation":[{"name":"Laboratory of Cell Biology, National Heart, Lung, and Blood Institute, National Institutes of 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