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Vol. 12, Issue 7, 1925-1935, July 2001
Subunit of the AP-1 Adaptor Complex Binds Clathrin:
Implications for Cooperative Binding in Coated Vesicle Assembly
Washington University School of Medicine, Department of Internal
Medicine, St. Louis, Missouri 63110
The heterotetrameric AP-1 adaptor complex is involved in the
assembly of clathrin-coated vesicles originating from the
trans-Golgi network (TGN). The 
1 subunit of AP-1 is
known to contain a consensus clathrin binding sequence, LLNLD (the
so-called clathrin box motif), in its hinge segment through which the
chain interacts with the N-terminal domains of clathrin trimers.
Here, we report that the hinge region of the 
subunit of human and
mouse AP-1 contains two copies of a new variant, LLDLL, of the clathrin
box motif that also bind to the terminal domain of the clathrin heavy
chain. High-affinity binding of the hinge to clathrin trimers
requires both LLDLL sequences to be present and the spacing between
them to be maintained. We also identify an independent clathrin-binding site within the appendage domain of the subunit that interacts with
a region of clathrin other than the N-terminal domain. Clathrin polymerization is promoted by glutathione S-transferase
(GST)- hinge, but not by GST- appendage. However, the
hinge and appendage domains of function in a cooperative manner to
recruit and polymerize clathrin, suggesting that clathrin lattice
assembly at the TGN involves multivalent binding of clathrin by the and 1 subunits of AP-1.
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