A key centriole assembly interaction interface between human Plk4 and STIL appears to not be conserved in flies
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 dom...
| Huvudupphovsmän: | , , , |
|---|---|
| Materialtyp: | Journal article |
| Språk: | English |
| Publicerad: |
Company of Biologists
2017
|
| _version_ | 1826276963610787840 |
|---|---|
| author | Cottee, M Johnson, S Raff, J Lea, S |
| author_facet | Cottee, M Johnson, S Raff, J Lea, S |
| author_sort | Cottee, M |
| collection | OXFORD |
| description | 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. |
| first_indexed | 2024-03-06T23:21:45Z |
| format | Journal article |
| id | oxford-uuid:68f4e696-3370-485c-bbb1-6e34a020beaf |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T23:21:45Z |
| publishDate | 2017 |
| publisher | Company of Biologists |
| record_format | dspace |
| spelling | oxford-uuid:68f4e696-3370-485c-bbb1-6e34a020beaf2022-03-26T18:48:23ZA key centriole assembly interaction interface between human Plk4 and STIL appears to not be conserved in fliesJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:68f4e696-3370-485c-bbb1-6e34a020beafEnglishSymplectic Elements at OxfordCompany of Biologists2017Cottee, MJohnson, SRaff, JLea, SA 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. |
| spellingShingle | Cottee, M Johnson, S Raff, J Lea, S A key centriole assembly interaction interface between human Plk4 and STIL appears to not be conserved in flies |
| title | A key centriole assembly interaction interface between human Plk4 and STIL appears to not be conserved in flies |
| title_full | A key centriole assembly interaction interface between human Plk4 and STIL appears to not be conserved in flies |
| title_fullStr | A key centriole assembly interaction interface between human Plk4 and STIL appears to not be conserved in flies |
| title_full_unstemmed | A key centriole assembly interaction interface between human Plk4 and STIL appears to not be conserved in flies |
| title_short | A key centriole assembly interaction interface between human Plk4 and STIL appears to not be conserved in flies |
| title_sort | key centriole assembly interaction interface between human plk4 and stil appears to not be conserved in flies |
| work_keys_str_mv | AT cotteem akeycentrioleassemblyinteractioninterfacebetweenhumanplk4andstilappearstonotbeconservedinflies AT johnsons akeycentrioleassemblyinteractioninterfacebetweenhumanplk4andstilappearstonotbeconservedinflies AT raffj akeycentrioleassemblyinteractioninterfacebetweenhumanplk4andstilappearstonotbeconservedinflies AT leas akeycentrioleassemblyinteractioninterfacebetweenhumanplk4andstilappearstonotbeconservedinflies AT cotteem keycentrioleassemblyinteractioninterfacebetweenhumanplk4andstilappearstonotbeconservedinflies AT johnsons keycentrioleassemblyinteractioninterfacebetweenhumanplk4andstilappearstonotbeconservedinflies AT raffj keycentrioleassemblyinteractioninterfacebetweenhumanplk4andstilappearstonotbeconservedinflies AT leas keycentrioleassemblyinteractioninterfacebetweenhumanplk4andstilappearstonotbeconservedinflies |