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Published 27 October 2003. doi:10.1083/jcb.200304079
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© The Rockefeller University Press, 0021-9525/2003/10/231 $8.00
The Journal of Cell Biology, Volume 163, Number 2, 231-236

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Clathrin promotes incorporation of cargo into coated pits by activation of the AP2 adaptor µ2 kinase



Antony P. Jackson1, Alexander Flett2,3, Carl Smythe2,3, Lindsay Hufton1, Frank R. Wettey1 and Elizabeth Smythe2,3

1 Department of Biochemistry, University of Cambridge, Cambridge CB2 1TN, England, UK
2 School of Life Sciences, University of Dundee, Dundee DD1 4HN, Scotland, UK
3 Department of Biomedical Sciences, University of Sheffield, Sheffield S10 2TN, England, UK

Address correspondence to Elizabeth Smythe, Dept. of Biomedical Sciences, University of Sheffield, Sheffield S10 2TN, England, UK. Tel.: 44-114-222-4635. Fax: 44-114-222-2788. email: e.smythe{at}sheffield.ac.uk

Endocytic cargo such as the transferrin receptor is incorporated into clathrin-coated pits by associating, via tyrosine-based motifs, with the AP2 complex. Cargo–AP2 interactions occur via the µ2 subunit of AP2, which needs to be phosphorylated for endocytosis to occur. The most likely role for µ2 phosphorylation is in cargo recruitment because µ2 phosphorylation enhances its binding to internalization motifs. Here, we investigate the control of µ2 phosphorylation. We identify clathrin as a specific activator of the µ2 kinase and, in permeabilized cells, we show that ligand sequestration, driven by exogenous clathrin, results in elevated levels of µ2 phosphorylation. Furthermore, we show that AP2 containing phospho-µ2 is mainly associated with assembled clathrin in vivo, and that the level of phospho-µ2 is strongly reduced in a chicken B cell line depleted of clathrin heavy chain. Our results imply a central role for clathrin in the regulation of cargo selection via the modulation of phospho-µ2 levels.

Key Words: regulation; endocytosis; sorting; coated vesicles; phosphorylation

A.P. Jackson and A. Flett contributed equally to this paper.


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