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| | ==Solution structure of the conserved C-terminal dimerization domain of Borealin== | | ==Solution structure of the conserved C-terminal dimerization domain of Borealin== |
| - | <StructureSection load='2kdd' size='340' side='right'caption='[[2kdd]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | + | <StructureSection load='2kdd' size='340' side='right'caption='[[2kdd]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2kdd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KDD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KDD FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2kdd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KDD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KDD FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CDCA8, PESCRG3 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2kdd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kdd OCA], [https://pdbe.org/2kdd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kdd RCSB], [https://www.ebi.ac.uk/pdbsum/2kdd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kdd ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2kdd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2kdd OCA], [https://pdbe.org/2kdd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2kdd RCSB], [https://www.ebi.ac.uk/pdbsum/2kdd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2kdd ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/BOREA_HUMAN BOREA_HUMAN]] Component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. In the complex, it may be required to direct the CPC to centromeric DNA. Major effector of the TTK kinase in the control of attachment-error-correction and chromosome alignment.<ref>PMID:15260989</ref> <ref>PMID:15249581</ref> <ref>PMID:16571674</ref> <ref>PMID:18243099</ref>
| + | [https://www.uniprot.org/uniprot/BOREA_HUMAN BOREA_HUMAN] Component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. In the complex, it may be required to direct the CPC to centromeric DNA. Major effector of the TTK kinase in the control of attachment-error-correction and chromosome alignment.<ref>PMID:15260989</ref> <ref>PMID:15249581</ref> <ref>PMID:16571674</ref> <ref>PMID:18243099</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bourhis, E]] | + | [[Category: Bourhis E]] |
| - | [[Category: Cochran, A G]] | + | [[Category: Cochran AG]] |
| - | [[Category: Fairbrother, W J]] | + | [[Category: Fairbrother WJ]] |
| - | [[Category: Lingel, A]] | + | [[Category: Lingel A]] |
| - | [[Category: Cell cycle]]
| + | |
| - | [[Category: Cell division]]
| + | |
| - | [[Category: Centromere]]
| + | |
| - | [[Category: Chromosomal protein]]
| + | |
| - | [[Category: Cytoplasm]]
| + | |
| - | [[Category: Mitosis]]
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| - | [[Category: Nucleus]]
| + | |
| - | [[Category: Phosphoprotein]]
| + | |
| - | [[Category: Polymorphism]]
| + | |
| - | [[Category: Protein dimer]]
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| Structural highlights
Function
BOREA_HUMAN Component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. In the complex, it may be required to direct the CPC to centromeric DNA. Major effector of the TTK kinase in the control of attachment-error-correction and chromosome alignment.[1] [2] [3] [4]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The chromosomal passenger complex (CPC) has been identified as a master regulator of mitosis. In particular, proper chromosome segregation and cytokinesis depend on the correct localization and function of the CPC. Within the complex, the kinase Aurora B associates with Incenp, Survivin and Borealin. The stoichiometry of the complex as well as a complete understanding of how these four components interact with each other remains to be elucidated. Here, we identify a new domain of Borealin. We determined its structure using NMR spectroscopy and discovered a novel dimerization motif. Interestingly, we found that substitutions at Borealin T230, recently identified as an Mps1 phosphorylation site, can modulate the dimerization state of Borealin. Mutation of this single residue to alanine or valine impairs Aurora B activity during mitosis and causes chromosome segregation defects. This study reveals that Mps1 regulates the CPC through a novel Borealin domain.
Phosphorylation of a Borealin dimerization domain is required for proper chromosome segregation.,Bourhis E, Lingel A, Phung Q, Fairbrother WJ, Cochran AG Biochemistry. 2009 Jun 17. PMID:19530738[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Sampath SC, Ohi R, Leismann O, Salic A, Pozniakovski A, Funabiki H. The chromosomal passenger complex is required for chromatin-induced microtubule stabilization and spindle assembly. Cell. 2004 Jul 23;118(2):187-202. PMID:15260989 doi:http://dx.doi.org/10.1016/j.cell.2004.06.026
- ↑ Gassmann R, Carvalho A, Henzing AJ, Ruchaud S, Hudson DF, Honda R, Nigg EA, Gerloff DL, Earnshaw WC. Borealin: a novel chromosomal passenger required for stability of the bipolar mitotic spindle. J Cell Biol. 2004 Jul 19;166(2):179-91. Epub 2004 Jul 12. PMID:15249581 doi:http://dx.doi.org/10.1083/jcb.200404001
- ↑ Klein UR, Nigg EA, Gruneberg U. Centromere targeting of the chromosomal passenger complex requires a ternary subcomplex of Borealin, Survivin, and the N-terminal domain of INCENP. Mol Biol Cell. 2006 Jun;17(6):2547-58. Epub 2006 Mar 29. PMID:16571674 doi:http://dx.doi.org/10.1091/mbc.E05-12-1133
- ↑ Jelluma N, Brenkman AB, van den Broek NJ, Cruijsen CW, van Osch MH, Lens SM, Medema RH, Kops GJ. Mps1 phosphorylates Borealin to control Aurora B activity and chromosome alignment. Cell. 2008 Jan 25;132(2):233-46. doi: 10.1016/j.cell.2007.11.046. PMID:18243099 doi:10.1016/j.cell.2007.11.046
- ↑ Bourhis E, Lingel A, Phung Q, Fairbrother WJ, Cochran AG. Phosphorylation of a Borealin dimerization domain is required for proper chromosome segregation. Biochemistry. 2009 Jun 17. PMID:19530738 doi:10.1021/bi900530v
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