Journal article
A key centriole assembly interaction interface between human Plk4 and STIL appears to not be conserved in flies
- Abstract:
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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 preclu...
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- Publication status:
- Published
- Peer review status:
- Peer reviewed
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(Version of record, pdf, 4.6MB)
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- Publisher copy:
- 10.1242/bio.024661
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Authors
Funding
+ Wellcome Trust
More from this funder
Funding agency for:
Raff, J
Grant:
Senior Investigator
Award 104575/Z/14/Z
+ Wellcome Trust
More from this funder
Funding agency for:
Lea, S
Grant:
Senior Investigator
Award 100298/Z/12/Z
Bibliographic Details
- Publisher:
- Company of Biologists Publisher's website
- Journal:
- Biology Open Journal website
- Volume:
- 6
- Issue:
- 3
- Pages:
- 381-389
- Publication date:
- 2017-02-15
- DOI:
- ISSN:
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2046-6390
Item Description
- Language:
- English
- Keywords:
- Pubs id:
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pubs:680831
- UUID:
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uuid:68f4e696-3370-485c-bbb1-6e34a020beaf
- Local pid:
- pubs:680831
- Deposit date:
- 2017-02-22
Terms of use
- Copyright holder:
- Cottee et al
- Copyright date:
- 2017
- Notes:
-
Copyright © 2017. Published by The Company of Biologists Ltd http://creativecommons.org/licenses/by/3.0
This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0), which permits unrestricted use, distribution and reproduction in any medium provided that the original work is properly attributed.
- Licence:
- CC Attribution (CC BY)
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