The γ-tubulin complex (γTuC) has a major role in microtubule (MT) nucleation at the centrosome and MT-organizing centres. Although this essential function is highly conserved in eukaryotes, the subunit composition of γTuC can vary depending on species or tissue. In most animals, γTuCs can consist of γ-tubulin, γ-complex-associated proteins 2 to 6 (GCP2–GCP6) and the small protein MOZART1. However, orthologs of GCP4–GCP6 have not been found in the common model organism Caenorhabditis elegans, despite requirements for γTuC in various tissues. In this study (Haruta et al., 2023), Asako Sugimoto and colleagues identify two previously uncharacterized proteins in C. elegans that associate with and regulate γTuC – the γ-tubulin-associated proteins GTAP-1 and -2. Both recruit γ-tubulin to centrosomes and influence the integrity of the pericentriolar matrix in C. elegans embryos, and GTAP-1, but not GTAP-2, is necessary for MT organisation at the plasma membrane in adult germline cells. Interestingly, GTAP-1 and -2 recruit γ-tubulin and other γTuC subunits in a different manner to MOZART1, and do not seem to have homology with GCP4–GCP6. A new phylogenetic analysis of C. elegans γTuC proteins suggests that ancient nematode worms might have lost the genes for GCP4–GCP6, creating selective pressure for evolution of divergent γTuC components. The discovery of these unconventional subunits might thus explain several unique properties of MTs found in C. elegans.