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15-Aug-2019 12:07

By analogy, these studies suggest that Ca M and Ca M-binding proteins might be required for centrosome-mediated microtubule nucleation by tethering γTu RC to centrosomes in animal cells.Consistent with this idea, two mammalian centrosome proteins, Kendrin (also called pericentrin B) and CG-NAP (also called AKAP350 or AKAP450), were found to contain Ca M binding motifs homologous to Spc110 ().

Thus far, other than the mammalian centriolar tubulin, only one mammalian centrosome protein, the outer dense fiber 2, has been shown to remain in the centrosome scaffold after high salt extraction (), two similar assays have been developed to study the microtubule-nucleating activity of the centrosome.These findings suggest that the microtubule-nucleating activity of the centrosome requires the function of CP309.We report the identification in k Da (CP309), cofractionates with the γ-tubulin ring complex and the centrosome-complementing activity.The centrosome, consisting of a pair of centrioles and a pericentriolar material, provides the major microtubule-nucleating function in animal cells ().


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Structural and biochemical studies have revealed that the pericentriolar material, which harbors the microtubule-nucleating activity, consists of a matrix-like structure (also referred to as the centrosome scaffold) and hundreds of γ-tubulin ring complexes (γTu RCs) ().We show that CP309 is required for microtubule nucleation mediated by centrosomes and that it interacts with the γ-tubulin small complex.