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A key centriole assembly interaction interface between human Plk4 and STIL appears to not be conserved in flies

Abstract:

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
Version:
Publisher's version

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Publisher copy:
10.1242/bio.024661

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Department:
Oxford, MSD, Pathology Dunn School
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Author
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Department:
Lincoln College
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Author
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Department:
Oxford, MSD, Pathology Dunn School
Role:
Author
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Funding agency for:
Raff, J
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Funding agency for:
Lea, SM
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:
2046-6390
Pubs id:
pubs:680831
URN:
uri:68f4e696-3370-485c-bbb1-6e34a020beaf
UUID:
uuid:68f4e696-3370-485c-bbb1-6e34a020beaf
Local pid:
pubs:680831
Paper number:
3
Language:
English
Keywords:

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