BETA-3A-ADAPTIN, A SUBUNIT OF THE ADAPTER-LIKE COMPLEX AP-3

Recent studies have described a widely expressed adaptor-like complex, named AP-3, which is likely involved in protein sorting in exocytic/e ndocytic pathways. The AP-3 complex is composed of four distinct subun its. Here, we report the identification of one of the subunits of this complex, which we call beta 3A-adaptin. The predicted amino acid sequ ence of beta 3A-adaptin reveals that the protein is closely related to the neuron-specific protein beta-NAP (61% overall identity) and more distantly related to the beta 1- and beta 2-adaptin subunits of the cl athrin-associated adaptor complexes AP-1 and AP-2, respectively. Seque nce comparisons also suggest that: beta 3A-adaptin has a domain organi zation similar to beta-NAP and to beta 1- and beta 2-adaptins, beta 3A -adaptin is expressed in all tissues and cells examined. Go-purificati on and co-precipitation analysesdemonstrate that beta 3A-adaptin corre sponds to the similar to 140-kDa subunit of the ubiquitous AP-3 comple x, the other subunits being delta-adaptin, p47A (now called mu 3A) and sigma 3 (A or 8). beta 3A-adaptin is phosphorylated on serine residue s in vivo while the other subunits of the complex are not detectably p hosphorylated, beta 3A-adaptin is not present in significant amounts i n clathrin-coated vesicles, The characteristics of beta 3A-adaptin rep orted here lend support to the idea that AP-3 is a structural and func tional homolog of the clathrin-associated adaptors AP-1 and AP-2.