Epithelia are composed of cells that are polarised locally (e.g. apico-basolateral axis establishment at the cellular level) and globally (e.g. coordination of axes across the tissue). Although polarity proteins are widely conserved, the mechanisms behind these programs are complex. Jessica Feldman and colleagues now investigate how polarity is established in the Caenorhabditis elegans intestinal epithelium. Using tissue-specific depletion and live imaging of endogenously tagged polarity proteins, the authors show that the apical surface is established first locally and then globally. Later, basolateral polarity proteins are gradually restricted to basolateral surfaces. They show that the apical polarity proteins PAR-3 and PKC-3 play different roles in polarisation. PKC-3 is dispensable for the establishment of apico-basolateral polarity but is required to maintain a continuous apical surface. Conversely, PAR-3 is necessary for global polarity establishment, but aspects of local polarity are eventually established in PAR-3-depleted intestines, indicated by the correct relative organisation of apical and basolateral proteins. Furthermore, local polarity in PAR-3-deficient intestines depends on HMR-1, the homolog of the adhesion protein E-cadherin. Together, these data show that the mechanisms involved in global and local polarity can be uncoupled, as PAR-3 is required for establishing global polarity but aspects of local polarity eventually arise without PAR-3.