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(Received for publication, February 24, 1997, and in revised form, April 18, 1997)
From the Cell Biology and Metabolism Branch, NICHD, National
Institutes of Health, Bethesda, Maryland 20892
Recent studies have described a widely expressed
adaptor-like complex, named AP-3, which is likely involved in protein
sorting in exocytic/endocytic pathways. The AP-3 complex is composed of four distinct subunits. Here, we report the identification of one of
the subunits of this complex, which we call
Volume 272, Number 24,
Issue of June 13, 1997
pp. 15078-15084
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
3A-adaptin, a Subunit of the Adaptor-like Complex AP-3
3A-adaptin. The
predicted amino acid sequence of 3A-adaptin reveals that the protein
is closely related to the neuron-specific protein -NAP (61% overall
identity) and more distantly related to the 1- and 2-adaptin
subunits of the clathrin-associated adaptor complexes AP-1 and AP-2,
respectively. Sequence comparisons also suggest that 3A-adaptin has
a domain organization similar to -NAP and to 1- and
2-adaptins. 3A-adaptin is expressed in all tissues and cells
examined. Co-purification and co-precipitation analyses demonstrate
that 3A-adaptin corresponds to the ~140-kDa subunit of the
ubiquitous AP-3 complex, the other subunits being 
-adaptin, p47A
(now called µ3A) and 
3 (A or B). 3A-adaptin is phosphorylated
on serine residues in vivo while the other subunits of the
complex are not detectably phosphorylated. 3A-adaptin is not present
in significant amounts in clathrin-coated vesicles. The characteristics
of 3A-adaptin reported here lend support to the idea that AP-3 is a
structural and functional homolog of the clathrin-associated adaptors
AP-1 and AP-2.
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