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of modeled with experimentally defined interactions of the vertebrate TACC proteins\nThe interaction data for the vertebrate TACCs is relatively limited; however, interaction networks are now beginning to emerge. The results of our functional analysis, as well as other published data clearly indicate that the vertebrate TACCs interact with proteins that can be divided into two broad categories: 1) proteins with roles in centrosome/mitotic spindle dynamics, and 2) proteins involved in gene regulation, either at the level of transcription, or subsequent RNA processing and translation [3,5-7,15,19-21,24,25,33,34]. Many of these proteins do not appear to interact directly with the protostome TACCs, but would be expected to be in the same protein complex (Fig. 6C,6D).\nSignificant 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].\nTo further characterize the evolving functions of the TACC proteins, we have used an unbiased yeast two hybrid screening method to identify proteins that bind to the human TACC proteins [3,34]. In a screen of a MATCHMAKER fetal brain library (BD Biosciences Clontech), in addition to isolating the histone acetyltransferase hGCN5L2 [34], we also identified the β3 isoform of retinoid-X receptor β as a protein that interacts with the TACC domain of TACC2. As shown in Fig. 7, this interaction is confirmed in vitro by GST-pull down analysis. Significantly, RXRβ is a close family relative of the nuclear hormone receptor, nhr-86, from C. elegans, which interacts with the ceTAC binding protein lin36 (Fig. 6A). This suggests that while protostome TACCs may require additional protein factors to interact with such components, the TACCs in higher organisms may have evolved the ability to directly interact with some of the proteins in the predicted interaction map (Fig. 6E). Indeed, this appears to be directly linked to the acquisition of new domains and duplication of the chordate TACC precursor. In fact, the first identified function of a vertebrate TACC protein was as a transcriptional coactivator acting through a direct interaction with the ARNT transcription factor [7]. It is also intriguing that the deuterostome specific SDP repeat interacts with GAS41, a component/accessory factor of the human SWI/SNF chromatin remodeling complex [3,15]. Although there is a D. melanogaster homologue of GAS41, dmGAS41, the large scale proteomic interaction database does not indicate a direct interaction of dmGAS41 with DTACC. This may be due to the lack of the SDP repeat region in the Drosophila TACC protein. This further suggests that the vertebrate TACCs have gained the specific ability to direct interact with transcriptional regulatory complexes, and that bridging protein(s) are no longer required. Thus, where the ceTAC protein is only composed of the TACC domain, the significantly larger TACC family members in higher protostomes and deuterostomes may have integrated one or more functions of the bridging protein (in this case lin15A, lin36 or lin37). This may also explain the absence of lin15A, lin36 and lin37 homologues in higher organisms, as they were no longer under selective evolutionary pressure to remain within the complex, and thus lost in the evolving genome.\nFigure 7 In vitro interaction of RXRβ3 and TACC2s. Top panel: Autoradiograph of 12% SDS polyacrylamide gel with in vitro translated RXRβ3 construct pulled down with GST-TACC2 (Lane 1) or GST (Lane 2); Lane 3: 5% input of in vitro translated RXR-β protein. Bottom two panels represent Coomassie blue stained gels of pull down experiment showing loading of GST-TACC2 and GST."}

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{"id":"T8324","span":{"begin":4245,"end":4250},"obj":"PR_EXT:000009822"},{"id":"T8325","span":{"begin":4290,"end":4296},"obj":"PR_EXT:Q27365"},{"id":"T8326","span":{"begin":4298,"end":4303},"obj":"PR_EXT:P34427"},{"id":"T8327","span":{"begin":4308,"end":4313},"obj":"PR_EXT:000009822"},{"id":"T8328","span":{"begin":4314,"end":4324},"obj":"SO_EXT:0000853"},{"id":"T8329","span":{"begin":4335,"end":4344},"obj":"NCBITaxon:1"},{"id":"T8330","span":{"begin":4428,"end":4435},"obj":"GO:0032991"},{"id":"T8331","span":{"begin":4467,"end":4473},"obj":"SO_EXT:0001026"},{"id":"T13860","span":{"begin":4519,"end":4525},"obj":"PR_EXT:000016007"},{"id":"T13861","span":{"begin":4560,"end":4563},"obj":"CHEBI:8984"},{"id":"T13862","span":{"begin":4564,"end":4578},"obj":"CHEBI_EXT:polyacrylamide"},{"id":"T13863","span":{"begin":4597,"end":4607},"obj":"GO:0006412"},{"id":"T13864","span":{"begin":4614,"end":4623},"obj":"SO_EXT:engineered_biological_sequence"},{"id":"T13865","span":{"begin":4641,"end":4644},"obj":"GO_PR_EXT:glutathione_S_transferase"},{"id":"T13866","span":{"begin":4645,"end":4650},"obj":"PR_EXT:000016007"},{"id":"T13867","span":{"begin":4663,"end":4666},"obj":"GO_PR_EXT:glutathione_S_transferase"},{"id":"T13868","span":{"begin":4706,"end":4716},"obj":"GO:0006412"},{"id":"T13869","span":{"begin":4717,"end":4720},"obj":"GO_EXT:0004886"},{"id":"T13870","span":{"begin":4717,"end":4722},"obj":"PR_EXT:000014373"},{"id":"T13871","span":{"begin":4723,"end":4730},"obj":"CHEBI_PR_EXT:protein"},{"id":"T13872","span":{"begin":4831,"end":4834},"obj":"GO_PR_EXT:glutathione_S_transferase"},{"id":"T13873","span":{"begin":4835,"end":4840},"obj":"PR_EXT:000016007"},{"id":"T13874","span":{"begin":4845,"end":4848},"obj":"GO_PR_EXT:glutathione_S_transferase"}],"relations":[{"id":"R5174","pred":"_lexicallyChainedTo","subj":"T8231","obj":"T8230"},{"id":"R5175","pred":"_lexicallyChainedTo","subj":"T8235","obj":"T8234"},{"id":"R5176","pred":"_lexicallyChainedTo","subj":"T8255","obj":"T8254"}],"text":"Comparison of modeled with experimentally defined interactions of the vertebrate TACC proteins\nThe interaction data for the vertebrate TACCs is relatively limited; however, interaction networks are now beginning to emerge. The results of our functional analysis, as well as other published data clearly indicate that the vertebrate TACCs interact with proteins that can be divided into two broad categories: 1) proteins with roles in centrosome/mitotic spindle dynamics, and 2) proteins involved in gene regulation, either at the level of transcription, or subsequent RNA processing and translation [3,5-7,15,19-21,24,25,33,34]. Many of these proteins do not appear to interact directly with the protostome TACCs, but would be expected to be in the same protein complex (Fig. 6C,6D).\nSignificant 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].\nTo further characterize the evolving functions of the TACC proteins, we have used an unbiased yeast two hybrid screening method to identify proteins that bind to the human TACC proteins [3,34]. In a screen of a MATCHMAKER fetal brain library (BD Biosciences Clontech), in addition to isolating the histone acetyltransferase hGCN5L2 [34], we also identified the β3 isoform of retinoid-X receptor β as a protein that interacts with the TACC domain of TACC2. As shown in Fig. 7, this interaction is confirmed in vitro by GST-pull down analysis. Significantly, RXRβ is a close family relative of the nuclear hormone receptor, nhr-86, from C. elegans, which interacts with the ceTAC binding protein lin36 (Fig. 6A). This suggests that while protostome TACCs may require additional protein factors to interact with such components, the TACCs in higher organisms may have evolved the ability to directly interact with some of the proteins in the predicted interaction map (Fig. 6E). Indeed, this appears to be directly linked to the acquisition of new domains and duplication of the chordate TACC precursor. In fact, the first identified function of a vertebrate TACC protein was as a transcriptional coactivator acting through a direct interaction with the ARNT transcription factor [7]. It is also intriguing that the deuterostome specific SDP repeat interacts with GAS41, a component/accessory factor of the human SWI/SNF chromatin remodeling complex [3,15]. Although there is a D. melanogaster homologue of GAS41, dmGAS41, the large scale proteomic interaction database does not indicate a direct interaction of dmGAS41 with DTACC. This may be due to the lack of the SDP repeat region in the Drosophila TACC protein. This further suggests that the vertebrate TACCs have gained the specific ability to direct interact with transcriptional regulatory complexes, and that bridging protein(s) are no longer required. Thus, where the ceTAC protein is only composed of the TACC domain, the significantly larger TACC family members in higher protostomes and deuterostomes may have integrated one or more functions of the bridging protein (in this case lin15A, lin36 or lin37). This may also explain the absence of lin15A, lin36 and lin37 homologues in higher organisms, as they were no longer under selective evolutionary pressure to remain within the complex, and thus lost in the evolving genome.\nFigure 7 In vitro interaction of RXRβ3 and TACC2s. Top panel: Autoradiograph of 12% SDS polyacrylamide gel with in vitro translated RXRβ3 construct pulled down with GST-TACC2 (Lane 1) or GST (Lane 2); Lane 3: 5% input of in vitro translated RXR-β protein. Bottom two panels represent Coomassie blue stained gels of pull down experiment showing loading of GST-TACC2 and GST."}

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of modeled with experimentally defined interactions of the vertebrate TACC proteins\nThe interaction data for the vertebrate TACCs is relatively limited; however, interaction networks are now beginning to emerge. The results of our functional analysis, as well as other published data clearly indicate that the vertebrate TACCs interact with proteins that can be divided into two broad categories: 1) proteins with roles in centrosome/mitotic spindle dynamics, and 2) proteins involved in gene regulation, either at the level of transcription, or subsequent RNA processing and translation [3,5-7,15,19-21,24,25,33,34]. Many of these proteins do not appear to interact directly with the protostome TACCs, but would be expected to be in the same protein complex (Fig. 6C,6D).\nSignificant 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].\nTo further characterize the evolving functions of the TACC proteins, we have used an unbiased yeast two hybrid screening method to identify proteins that bind to the human TACC proteins [3,34]. In a screen of a MATCHMAKER fetal brain library (BD Biosciences Clontech), in addition to isolating the histone acetyltransferase hGCN5L2 [34], we also identified the β3 isoform of retinoid-X receptor β as a protein that interacts with the TACC domain of TACC2. As shown in Fig. 7, this interaction is confirmed in vitro by GST-pull down analysis. Significantly, RXRβ is a close family relative of the nuclear hormone receptor, nhr-86, from C. elegans, which interacts with the ceTAC binding protein lin36 (Fig. 6A). This suggests that while protostome TACCs may require additional protein factors to interact with such components, the TACCs in higher organisms may have evolved the ability to directly interact with some of the proteins in the predicted interaction map (Fig. 6E). Indeed, this appears to be directly linked to the acquisition of new domains and duplication of the chordate TACC precursor. In fact, the first identified function of a vertebrate TACC protein was as a transcriptional coactivator acting through a direct interaction with the ARNT transcription factor [7]. It is also intriguing that the deuterostome specific SDP repeat interacts with GAS41, a component/accessory factor of the human SWI/SNF chromatin remodeling complex [3,15]. Although there is a D. melanogaster homologue of GAS41, dmGAS41, the large scale proteomic interaction database does not indicate a direct interaction of dmGAS41 with DTACC. This may be due to the lack of the SDP repeat region in the Drosophila TACC protein. This further suggests that the vertebrate TACCs have gained the specific ability to direct interact with transcriptional regulatory complexes, and that bridging protein(s) are no longer required. Thus, where the ceTAC protein is only composed of the TACC domain, the significantly larger TACC family members in higher protostomes and deuterostomes may have integrated one or more functions of the bridging protein (in this case lin15A, lin36 or lin37). This may also explain the absence of lin15A, lin36 and lin37 homologues in higher organisms, as they were no longer under selective evolutionary pressure to remain within the complex, and thus lost in the evolving genome.\nFigure 7 In vitro interaction of RXRβ3 and TACC2s. Top panel: Autoradiograph of 12% SDS polyacrylamide gel with in vitro translated RXRβ3 construct pulled down with GST-TACC2 (Lane 1) or GST (Lane 2); Lane 3: 5% input of in vitro translated RXR-β protein. Bottom two panels represent Coomassie blue stained gels of pull down experiment showing loading of GST-TACC2 and GST."}

{"project":"2_test","denotations":[{"id":"15207008-12620397-9666042","span":{"begin":600,"end":601},"obj":"12620397"},{"id":"15207008-12956952-9666043","span":{"begin":602,"end":603},"obj":"12956952"},{"id":"15207008-12956951-9666043","span":{"begin":602,"end":603},"obj":"12956951"},{"id":"15207008-11025203-9666043","span":{"begin":602,"end":603},"obj":"11025203"},{"id":"15207008-11903063-9666044","span":{"begin":606,"end":608},"obj":"11903063"},{"id":"15207008-12165861-9666045","span":{"begin":609,"end":611},"obj":"12165861"},{"id":"15207008-14603251-9666045","span":{"begin":609,"end":611},"obj":"14603251"},{"id":"15207008-14602875-9666045","span":{"begin":609,"end":611},"obj":"14602875"},{"id":"15207008-11433296-9666046","span":{"begin":615,"end":617},"obj":"11433296"},{"id":"15207008-11827981-9666047","span":{"begin":618,"end":620},"obj":"11827981"},{"id":"15207008-11847113-9666048","span":{"begin":621,"end":623},"obj":"11847113"},{"id":"15207008-14767476-9666049","span":{"begin":624,"end":626},"obj":"14767476"},{"id":"15207008-12956952-9666050","span":{"begin":943,"end":944},"obj":"12956952"},{"id":"15207008-12956951-9666051","span":{"begin":945,"end":946},"obj":"12956951"},{"id":"15207008-14602875-9666052","span":{"begin":947,"end":949},"obj":"14602875"},{"id":"15207008-12970190-9666052","span":{"begin":947,"end":949},"obj":"12970190"},{"id":"15207008-12569123-9666052","span":{"begin":947,"end":949},"obj":"12569123"},{"id":"15207008-11433296-9666052","span":{"begin":947,"end":949},"obj":"11433296"},{"id":"15207008-11121038-9666053","span":{"begin":1130,"end":1132},"obj":"11121038"},{"id":"15207008-14602875-9666054","span":{"begin":1270,"end":1272},"obj":"14602875"},{"id":"15207008-10635326-9666055","span":{"begin":1662,"end":1663},"obj":"10635326"},{"id":"15207008-11081630-9666056","span":{"begin":1664,"end":1666},"obj":"11081630"},{"id":"15207008-12165861-9666057","span":{"begin":2081,"end":2083},"obj":"12165861"},{"id":"15207008-12620397-9666058","span":{"begin":2273,"end":2274},"obj":"12620397"},{"id":"15207008-14767476-9666059","span":{"begin":2275,"end":2277},"obj":"14767476"},{"id":"15207008-14767476-9666060","span":{"begin":2419,"end":2421},"obj":"14767476"},{"id":"15207008-11025203-9666061","span":{"begin":3364,"end":3365},"obj":"11025203"},{"id":"15207008-12620397-9666062","span":{"begin":3534,"end":3535},"obj":"12620397"},{"id":"15207008-11903063-9666063","span":{"begin":3536,"end":3538},"obj":"11903063"}],"text":"Comparison of modeled with experimentally defined interactions of the vertebrate TACC proteins\nThe interaction data for the vertebrate TACCs is relatively limited; however, interaction networks are now beginning to emerge. The results of our functional analysis, as well as other published data clearly indicate that the vertebrate TACCs interact with proteins that can be divided into two broad categories: 1) proteins with roles in centrosome/mitotic spindle dynamics, and 2) proteins involved in gene regulation, either at the level of transcription, or subsequent RNA processing and translation [3,5-7,15,19-21,24,25,33,34]. Many of these proteins do not appear to interact directly with the protostome TACCs, but would be expected to be in the same protein complex (Fig. 6C,6D).\nSignificant 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].\nTo further characterize the evolving functions of the TACC proteins, we have used an unbiased yeast two hybrid screening method to identify proteins that bind to the human TACC proteins [3,34]. In a screen of a MATCHMAKER fetal brain library (BD Biosciences Clontech), in addition to isolating the histone acetyltransferase hGCN5L2 [34], we also identified the β3 isoform of retinoid-X receptor β as a protein that interacts with the TACC domain of TACC2. As shown in Fig. 7, this interaction is confirmed in vitro by GST-pull down analysis. Significantly, RXRβ is a close family relative of the nuclear hormone receptor, nhr-86, from C. elegans, which interacts with the ceTAC binding protein lin36 (Fig. 6A). This suggests that while protostome TACCs may require additional protein factors to interact with such components, the TACCs in higher organisms may have evolved the ability to directly interact with some of the proteins in the predicted interaction map (Fig. 6E). Indeed, this appears to be directly linked to the acquisition of new domains and duplication of the chordate TACC precursor. In fact, the first identified function of a vertebrate TACC protein was as a transcriptional coactivator acting through a direct interaction with the ARNT transcription factor [7]. It is also intriguing that the deuterostome specific SDP repeat interacts with GAS41, a component/accessory factor of the human SWI/SNF chromatin remodeling complex [3,15]. Although there is a D. melanogaster homologue of GAS41, dmGAS41, the large scale proteomic interaction database does not indicate a direct interaction of dmGAS41 with DTACC. This may be due to the lack of the SDP repeat region in the Drosophila TACC protein. This further suggests that the vertebrate TACCs have gained the specific ability to direct interact with transcriptional regulatory complexes, and that bridging protein(s) are no longer required. Thus, where the ceTAC protein is only composed of the TACC domain, the significantly larger TACC family members in higher protostomes and deuterostomes may have integrated one or more functions of the bridging protein (in this case lin15A, lin36 or lin37). This may also explain the absence of lin15A, lin36 and lin37 homologues in higher organisms, as they were no longer under selective evolutionary pressure to remain within the complex, and thus lost in the evolving genome.\nFigure 7 In vitro interaction of RXRβ3 and TACC2s. Top panel: Autoradiograph of 12% SDS polyacrylamide gel with in vitro translated RXRβ3 construct pulled down with GST-TACC2 (Lane 1) or GST (Lane 2); Lane 3: 5% input of in vitro translated RXR-β protein. Bottom two panels represent Coomassie blue stained gels of pull down experiment showing loading of GST-TACC2 and GST."}