Although polarized epithelial cells are well known to maintain distinct api
cal and basolateral plasma membrane domains, the mechanisms responsible for
targeting membrane proteins to the apical or basolateral surfaces have rem
ained elusive. We have identified a novel form of the AP-1 clathrin adaptor
complex that contains as one of its subunits mu 1B, an epithelial cell-spe
cific homolog of the ubiquitously expressed mu 1A. LLC-PK1 kidney epithelia
l cells do not express mu 1B and missort many basolateral proteins to the a
pical surface. Stable expression of mu 1B selectively restored basolateral
targeting, improved the overall organization of LLC-PK1 monolayers, and had
no effect on apical targeting. We conclude that basolateral sorting is med
iated by an epithelial cell-specific version of the AP-1 complex containing
mu 1B.