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J. Biol. Chem., Vol. 276, Issue 39, 36131-36138, September 28, 2001
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From the Department of Cell Biology, Center of Anatomy,
Hannover Medical School, D-30125 Hannover, Germany
The removal of the clathrin coat is
essential for vesicle fusion with acceptor membranes. Disassembly of
the coat involves hsc70, which is specifically recruited by members of
the auxilin protein family to clathrin lattices. In vitro,
this function of auxilin does not require the globular amino-terminal
domain of the clathrin heavy chain, which is known to play a prominent
role in the interaction of clathrin with adaptors and numerous
endocytic accessory proteins. Here we report the unexpected finding
that the neuron-specific form of auxilin (auxilin 1) can also associate with the clathrin amino-terminal domain. This interaction is mediated through tandemly arranged sites within the auxilin 1 carboxyl-terminal segment 547-910. The overlapping auxilin 1 fragments 547-714 and 619-738 bind the clathrin terminal domain with high affinity, whereas
auxilin 1-(715-901) interacts only poorly with it. All three fragments
also associate with the clathrin distal domain and the
Multiple Interactions of Auxilin 1 with Clathrin and the AP-2
Adaptor Complex*
-appendage
domain of AP-2. Moreover, they support efficient assembly of clathrin
triskelia into regular cages. A novel uncoating assay was developed to
demonstrate that auxilin 1-(715-901) functions efficiently as a
cofactor for hsc70 in the uncoating of clathrin-coated vesicles. The
multiple protein-protein interactions of auxilin 1 suggest that its
function in endocytic trafficking may be more complex than previously anticipated.
*
This work was supported by the German Research Foundation.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.:
49-511-532-6744; Fax: 49-511-532-3903; E-mail:
ungewickell.ernst@mh-hannover.de.
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