The centrosome serves as the major microtubule-nucleating and - organizing center in animal cells. It is composed of hundreds of proteins. The molecular details of how centrosomal proteins contribute to centrotome function are only beginning to emerge. Members of the neuron-precursor-cell-expressed developmentally downregulated protein 1 (NEDD1) family of conserved proteins have recently been implicated in recruiting gamma-tubulin and its associated proteins, which together make up the gamma-tubulin ring complex (gamma TuRC), to the centrosome. Human NEDD1 and its Drosophila ortholog Dgp71WD are WD-repeat proteins that interact with the gamma TuRC. Experimental knockdown of human NEDD1 was recently shown to result in loss of gamma-tubulin from the centrosome. By contrast, however, Dgp71WD knockdown has no effect on targeting the gamma TuRC to the centrosome in flies. Using Xenopus egg extracts, we show that Xenopus NEDD1 is mostly dispensable for targeting gamma-tubulin to centrosomes, but that microtubule organization is disrupted in NEDD1-depleted extracts. We show that NEDD1 exists in a complex that is distinct from the gamma TuRC, suggesting that NEDD1 may not be a bona fide subunit of the Xenopus gamma TuRC. We propose that the main function of NEDD1 in Xenopus is in microtubule organization.