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Published 8 May 2006. doi:10.1083/jcb.200602054
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 173, Number 3, 443-452
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Article

 Drosophila melanogaster auxilin regulates the internalization of Delta to control activity of the Notch signaling pathway

Elliott J. Hagedorn, Jennifer L. Bayraktar, Vasundhara R. Kandachar, Ting Bai, Dane M. Englert, and Henry C. Chang

Department of Biological Sciences, Purdue University, West Lafayette, IN 47907

Correspondence to Henry C. Chang: hcchang{at}purdue.edu

We have isolated mutations in the Drosophila melanogaster homologue of auxilin, a J-domain–containing protein known to cooperate with Hsc70 in the disassembly of clathrin coats from clathrin-coated vesicles in vitro. Consistent with this biochemical role, animals with reduced auxilin function exhibit genetic interactions with Hsc70 and clathrin. Interestingly, the auxilin mutations interact specifically with Notch and disrupt several Notch-mediated processes. Genetic evidence places auxilin function in the signal-sending cells, upstream of Notch receptor activation, suggesting that the relevant cargo for this auxilin-mediated endocytosis is the Notch ligand Delta. Indeed, the localization of Delta protein is disrupted in auxilin mutant tissues. Thus, our data suggest that auxilin is an integral component of the Notch signaling pathway, participating in the ubiquitin-dependent endocytosis of Delta. Furthermore, the fact that auxilin is required for Notch signaling suggests that ligand endocytosis in the signal-sending cells needs to proceed past coat disassembly to activate Notch.

E.J. Hagedorn and J.L. Bayraktar contributed equally to this work.

Abbreviations used in this paper: CCV, clathrin-coated vesicle; Clc, clathrin light chain; Dl, Delta; DSL, Dl, Ser, and Caenorhabditis elegans Lag-2 protein family; EGFR, EGF receptor; NECD, Notch extracellular domain; Ser, Serrate; UAS, upstream activating sequence.


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