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Published online
doi:10.1083/jcb.200608033
The Journal of Cell Biology, Vol. 178, No. 3, 453-464
The Rockefeller University Press, 0021-9525 $30.00
© Li et al.
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Article

An ACAP1-containing clathrin coat complex for endocytic recycling



Jian Li1,2, Peter J. Peters5, Ming Bai1,2, Jun Dai1,2, Erik Bos5, Tomas Kirchhausen3,4, Konstantin V. Kandror6, and Victor W. Hsu1,2

1 Division of Rheumatology, Immunology, and Allergy, Brigham and Women's Hospital, Boston, MA 02115
2 Department of Medicine, 3 Department of Cell Biology, and 4 The CBR Institute for Biomedical Research, Harvard Medical School, Boston, MA 02115
5 Division of Cell Biology, Netherlands Cancer Institute, 1066 CX Amsterdam, Netherlands
6 Department of Biochemistry, Boston University School of Medicine, Boston, MA 02118

Correspondence to Victor Hsu: vhsu{at}rics.bwh.harvard.edu

Whether coat proteins play a widespread role in endocytic recycling remains unclear. We find that ACAP1, a GTPase-activating protein (GAP) for ADP-ribosylation factor (ARF) 6, is part of a novel clathrin coat complex that is regulated by ARF6 for endocytic recycling in two key physiological settings, stimulation-dependent recycling of integrin that is critical for cell migration and insulin-stimulated recycling of glucose transporter type 4 (Glut4), which is required for glucose homeostasis. These findings not only advance a basic understanding of an early mechanistic step in endocytic recycling but also shed key mechanistic insights into major physiological events for which this transport plays a critical role.

Abbreviations used in this paper: ACAP, ARFGAP with coiled coil, ANK repeat, and pleckstrin homology domains; AP, adaptor protein; ARF, ADP-ribosylation factor; CHC, clathrin heavy chain; COPI, coat protein I; EGFR, EGF receptor; GAP, GTPase-activating protein; Glut4, glucose transporter type 4; TfR, transferrin receptor; VSVG, vesicular stomatitis virus G protein.


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