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Vol. 10, Issue 8, 2787-2802, August 1999
University of Cambridge, Department of Clinical Biochemistry and
Cambridge Institute for Medical Research, Cambridge CB2 2XY, England
Adaptor protein complexes (APs) function as vesicle coat components
in different membrane traffic pathways; however, there are a number of
pathways for which there is still no candidate coat. To find novel coat
components related to AP complexes, we have searched the expressed
sequence tag database and have identified, cloned, and sequenced
a new member of each of the four AP subunit families. We have shown by
a combination of coimmunoprecipitation and yeast two-hybrid analysis
that these four proteins (
, 
4, µ4, and 
4) are components of
a novel adaptor-like heterotetrameric complex, which we are calling
AP-4. Immunofluorescence reveals that AP-4 is localized to ~10-20
discrete dots in the perinuclear region of the cell. This pattern is
disrupted by treating the cells with brefeldin A, indicating that, like
other coat proteins, the association of AP-4 with membranes is
regulated by the small GTPase ARF. Immunogold electron
microscopy indicates that AP-4 is associated with nonclathrin-coated
vesicles in the region of the trans-Golgi network. The µ4 subunit of
the complex specifically interacts with a tyrosine-based sorting
signal, indicating that, like the other three AP complexes, AP-4 is
involved in the recognition and sorting of cargo proteins with
tyrosine-based motifs. AP-4 is of relatively low abundance, but it is
expressed ubiquitously, suggesting that it participates in a
specialized trafficking pathway but one that is required in all cell types.
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