Polarisation of cell types such as neurons and epithelial cells involves localised plasma membrane growth, a process that requires the sorting and targeting of exocytic transport vesicles to the growth site. The Sec6/8 (exocyst) complex regulates vesicle delivery in many cell types but how it is localised is unclear? Charles Yeaman et al. have investigated this problem in polarised MDCK cells (see p. 559). They show that Sec6/8 is rapidly recruited from the cytosol to cell-cell contact sites when the cells begin to undergo E-cadherin-mediated adhesion. Subsequently, the complex is further sorted to the apex of the lateral membrane, where it associates with components of tight junctions and nectin complexes, the major binding partners for the Sec6/8 complex being E-cadherin and nectin 2a. Finally, to show that these associations are functionally important in the localisation of the Sec6/8 complex, the authors report that recruitment of the complex to cell-cell contacts can be driven in fibroblasts by co-expression of E-cadherin and nectin 2a.