Primary cilia fulfil important roles in nearly all cells and tissues and, consequently, defects in ciliogenesis or in cilia function are associated with a number of diseases. During ciliogenesis, cilia grow by extension of a microtubule core, the axoneme, and intraflagellar transport (IFT) provides the particles for cilia assembly. Dynein-2 is known to drive retrograde IFT along the axoneme and is also important for cilia formation. Furthermore, Golgi-localised proteins have also been implicated in ciliogenesis and IFT. In this work (p. 5189), David Stephens and colleagues now further investigate the molecular mechanisms of the involvement of Golgi proteins in ciliogenesis. By using RNA interference (RNAi), they show that the transmembrane Golgi matrix protein giantin (also known as GOLGB1) is required for ciliogenesis. Interestingly, they demonstrate that giantin does not act through the Rab11–Rabin–Rab8 pathway that has previously been suggested to be important for the early steps of ciliogenesis. Instead, they find that functional suppression of giantin leads to a mislocalisation of the dynein-2 intermediate chain WDR34. Accordingly, depletion of giantin or of WDR34 results in an inability of cells to form primary cilia, whereas their partial depletion increased cilia length. Taken together, the data presented here suggest that giantin acts in ciliogenesis by controlling the localization of dynein-2.