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analysis of the association of the TACCs with the centrosome and the dynamics of mitotic spindle assembly from yeast to humans has been published [5,6,21-24]. From this analysis, it seems likely that the vertebrate TACC3 protein has retained this direct ancestral function, based upon its location in these structures during mitosis [27], its strong interaction with Aurora Kinase A, and the observation that it is the only human TACC protein phosphorylated by this enzyme [21]. However, the variability of the central domain of the vertebrate orthologues, suggests that TACC3 may also have acquired additional, and in some instances, species-specific functions. For instance, in X. laevis, the maskin protein has acquired a binding site for the eIF4E protein, and thus a function in the coordinated control of polyadenylation and translation in the Xenopus oocyte [8,35]. A recent study has suggested that this function may be unique to maskin: although it is unclear whether the other vertebrate TACC3 proteins interact with the eIF4E/CPEB complex, the human TACC1A isoform is unable to interact with the eIF4E/CPEB complex. Instead, some TACC1 isoforms have evolved a related, but distinct function by directly interacting with elements of the RNA splicing and transport machinery [19]."}

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From this analysis, it seems likely that the vertebrate TACC3 protein has retained this direct ancestral function, based upon its location in these structures during mitosis [27], its strong interaction with Aurora Kinase A, and the observation that it is the only human TACC protein phosphorylated by this enzyme [21]. However, the variability of the central domain of the vertebrate orthologues, suggests that TACC3 may also have acquired additional, and in some instances, species-specific functions. For instance, in X. laevis, the maskin protein has acquired a binding site for the eIF4E protein, and thus a function in the coordinated control of polyadenylation and translation in the Xenopus oocyte [8,35]. A recent study has suggested that this function may be unique to maskin: although it is unclear whether the other vertebrate TACC3 proteins interact with the eIF4E/CPEB complex, the human TACC1A isoform is unable to interact with the eIF4E/CPEB complex. Instead, some TACC1 isoforms have evolved a related, but distinct function by directly interacting with elements of the RNA splicing and transport machinery [19]."}

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{"project":"2_test","denotations":[{"id":"15207008-12956952-9666050","span":{"begin":159,"end":160},"obj":"12956952"},{"id":"15207008-12956951-9666051","span":{"begin":161,"end":162},"obj":"12956951"},{"id":"15207008-14602875-9666052","span":{"begin":163,"end":165},"obj":"14602875"},{"id":"15207008-12970190-9666052","span":{"begin":163,"end":165},"obj":"12970190"},{"id":"15207008-12569123-9666052","span":{"begin":163,"end":165},"obj":"12569123"},{"id":"15207008-11433296-9666052","span":{"begin":163,"end":165},"obj":"11433296"},{"id":"15207008-11121038-9666053","span":{"begin":346,"end":348},"obj":"11121038"},{"id":"15207008-14602875-9666054","span":{"begin":486,"end":488},"obj":"14602875"},{"id":"15207008-10635326-9666055","span":{"begin":878,"end":879},"obj":"10635326"},{"id":"15207008-11081630-9666056","span":{"begin":880,"end":882},"obj":"11081630"},{"id":"15207008-12165861-9666057","span":{"begin":1297,"end":1299},"obj":"12165861"}],"text":"Significant analysis of the association of the TACCs with the centrosome and the dynamics of mitotic spindle assembly from yeast to humans has been published [5,6,21-24]. From this analysis, it seems likely that the vertebrate TACC3 protein has retained this direct ancestral function, based upon its location in these structures during mitosis [27], its strong interaction with Aurora Kinase A, and the observation that it is the only human TACC protein phosphorylated by this enzyme [21]. However, the variability of the central domain of the vertebrate orthologues, suggests that TACC3 may also have acquired additional, and in some instances, species-specific functions. For instance, in X. laevis, the maskin protein has acquired a binding site for the eIF4E protein, and thus a function in the coordinated control of polyadenylation and translation in the Xenopus oocyte [8,35]. A recent study has suggested that this function may be unique to maskin: although it is unclear whether the other vertebrate TACC3 proteins interact with the eIF4E/CPEB complex, the human TACC1A isoform is unable to interact with the eIF4E/CPEB complex. Instead, some TACC1 isoforms have evolved a related, but distinct function by directly interacting with elements of the RNA splicing and transport machinery [19]."}