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| | ==PB3 Domain of Drosophila melanogaster PLK4 (Sak)== | | ==PB3 Domain of Drosophila melanogaster PLK4 (Sak)== |
| - | <StructureSection load='5lhx' size='340' side='right' caption='[[5lhx]], [[Resolution|resolution]] 1.53Å' scene=''> | + | <StructureSection load='5lhx' size='340' side='right'caption='[[5lhx]], [[Resolution|resolution]] 1.53Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5lhx]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LHX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LHX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5lhx]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5LHX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5LHX FirstGlance]. <br> |
| - | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Polo_kinase Polo kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.11.21 2.7.11.21] </span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.53Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5lhx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lhx OCA], [http://pdbe.org/5lhx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lhx RCSB], [http://www.ebi.ac.uk/pdbsum/5lhx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lhx 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=5lhx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lhx OCA], [https://pdbe.org/5lhx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5lhx RCSB], [https://www.ebi.ac.uk/pdbsum/5lhx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5lhx ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PLK4_DROME PLK4_DROME]] Serine/threonine-protein kinase that plays a central role in centriole duplication. Able to trigger procentriole formation on the surface of the mother centriole cylinder, using mother centriole as a platform, leading to the recruitment of centriole biogenesis proteins such as Sas-6. When overexpressed, it is able to induce centrosome amplification through the simultaneous generation of multiple procentrioles adjoining each parental centriole during S phase. Centrosome amplification following overexpression can initiate tumorigenesis, highlighting the importance of centrosome regulation in cancers.<ref>PMID:16326102</ref> <ref>PMID:17463247</ref> <ref>PMID:18555779</ref> | + | [https://www.uniprot.org/uniprot/PLK4_DROME PLK4_DROME] Serine/threonine-protein kinase that plays a central role in centriole duplication. Able to trigger procentriole formation on the surface of the mother centriole cylinder, using mother centriole as a platform, leading to the recruitment of centriole biogenesis proteins such as Sas-6. When overexpressed, it is able to induce centrosome amplification through the simultaneous generation of multiple procentrioles adjoining each parental centriole during S phase. Centrosome amplification following overexpression can initiate tumorigenesis, highlighting the importance of centrosome regulation in cancers.<ref>PMID:16326102</ref> <ref>PMID:17463247</ref> <ref>PMID:18555779</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5lhx" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5lhx" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Serine/threonine protein kinase 3D structures|Serine/threonine protein kinase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Polo kinase]] | + | [[Category: Drosophila melanogaster]] |
| - | [[Category: Cottee, M A]] | + | [[Category: Large Structures]] |
| - | [[Category: Lea, S M]] | + | [[Category: Cottee MA]] |
| - | [[Category: Centriole]] | + | [[Category: Lea SM]] |
| - | [[Category: Polo box domain]]
| + | |
| - | [[Category: Structural protein]]
| + | |
| - | [[Category: Transferase]]
| + | |
| Structural highlights
Function
PLK4_DROME Serine/threonine-protein kinase that plays a central role in centriole duplication. Able to trigger procentriole formation on the surface of the mother centriole cylinder, using mother centriole as a platform, leading to the recruitment of centriole biogenesis proteins such as Sas-6. When overexpressed, it is able to induce centrosome amplification through the simultaneous generation of multiple procentrioles adjoining each parental centriole during S phase. Centrosome amplification following overexpression can initiate tumorigenesis, highlighting the importance of centrosome regulation in cancers.[1] [2] [3]
Publication Abstract from PubMed
A small number of proteins form a conserved pathway of centriole duplication. In humans and flies, the binding of Plk4/Sak to STIL/Ana2 initiates daughter centriole assembly. In humans, this interaction is mediated by an interaction between the Polo-Box-3 (PB3) domain of Plk4 and the coiled-coil domain of STIL (HsCCD). We showed previously that the Drosophila Ana2 coiled-coil domain (DmCCD) is essential for centriole assembly, but it forms a tight parallel tetramer in vitro that likely precludes an interaction with PB3. Here we show that the isolated HsCCD and HsPB3 domains form a mixture of homo-multimers in vitro, but these readily dissociate when mixed to form the previously described 1:1 HsCCD:HsPB3 complex. In contrast, although Drosophila PB3 (DmPB3) adopts a canonical polo-box fold, it does not detectably interact with DmCCD in vitro Thus, surprisingly, a key centriole assembly interaction interface appears to differ between humans and flies.
A key centriole assembly interaction interface between human Plk4 and STIL appears to not be conserved in flies.,Cottee MA, Johnson S, Raff JW, Lea SM Biol Open. 2017 Feb 15. pii: bio.024661. doi: 10.1242/bio.024661. PMID:28202467[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bettencourt-Dias M, Rodrigues-Martins A, Carpenter L, Riparbelli M, Lehmann L, Gatt MK, Carmo N, Balloux F, Callaini G, Glover DM. SAK/PLK4 is required for centriole duplication and flagella development. Curr Biol. 2005 Dec 20;15(24):2199-207. Epub 2005 Dec 1. PMID:16326102 doi:http://dx.doi.org/10.1016/j.cub.2005.11.042
- ↑ Rodrigues-Martins A, Riparbelli M, Callaini G, Glover DM, Bettencourt-Dias M. Revisiting the role of the mother centriole in centriole biogenesis. Science. 2007 May 18;316(5827):1046-50. Epub 2007 Apr 26. PMID:17463247 doi:http://dx.doi.org/10.1126/science.1142950
- ↑ Basto R, Brunk K, Vinadogrova T, Peel N, Franz A, Khodjakov A, Raff JW. Centrosome amplification can initiate tumorigenesis in flies. Cell. 2008 Jun 13;133(6):1032-42. doi: 10.1016/j.cell.2008.05.039. PMID:18555779 doi:http://dx.doi.org/10.1016/j.cell.2008.05.039
- ↑ Cottee MA, Johnson S, Raff JW, Lea SM. A key centriole assembly interaction interface between human Plk4 and STIL appears to not be conserved in flies. Biol Open. 2017 Feb 15. pii: bio.024661. doi: 10.1242/bio.024661. PMID:28202467 doi:http://dx.doi.org/10.1242/bio.024661
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