Direct binding of CEP85 to STIL ensures robust PLK4 activation and efficient centriole assembly

Centriole duplication is tightly regulated in vivo, but the underlying molecular mechanisms are incompletely understood. Here the authors use high-resolution structural and imaging methods to show that CEP85 directly interacts with STIL and mediates efficient centriolar targeting of STIL, PLK4 activ...

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Autores principales:	Yi Liu, Gagan D. Gupta, Deepak D. Barnabas, Fikret G. Agircan, Shahid Mehmood, Di Wu, Etienne Coyaud, Christopher M. Johnson, Stephen H. McLaughlin, Antonina Andreeva, Stefan M. V. Freund, Carol V. Robinson, Sally W. T. Cheung, Brian Raught, Laurence Pelletier, Mark van Breugel
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/64d5bf6e3d9f4b17ae080b2ad6edfff9
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spelling	oai:doaj.org-article:64d5bf6e3d9f4b17ae080b2ad6edfff92021-12-02T16:49:52ZDirect binding of CEP85 to STIL ensures robust PLK4 activation and efficient centriole assembly10.1038/s41467-018-04122-x2041-1723https://doaj.org/article/64d5bf6e3d9f4b17ae080b2ad6edfff92018-04-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-04122-xhttps://doaj.org/toc/2041-1723Centriole duplication is tightly regulated in vivo, but the underlying molecular mechanisms are incompletely understood. Here the authors use high-resolution structural and imaging methods to show that CEP85 directly interacts with STIL and mediates efficient centriolar targeting of STIL, PLK4 activation and centriole assembly.Yi LiuGagan D. GuptaDeepak D. BarnabasFikret G. AgircanShahid MehmoodDi WuEtienne CoyaudChristopher M. JohnsonStephen H. McLaughlinAntonina AndreevaStefan M. V. FreundCarol V. RobinsonSally W. T. CheungBrian RaughtLaurence PelletierMark van BreugelNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-15 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Yi Liu Gagan D. Gupta Deepak D. Barnabas Fikret G. Agircan Shahid Mehmood Di Wu Etienne Coyaud Christopher M. Johnson Stephen H. McLaughlin Antonina Andreeva Stefan M. V. Freund Carol V. Robinson Sally W. T. Cheung Brian Raught Laurence Pelletier Mark van Breugel Direct binding of CEP85 to STIL ensures robust PLK4 activation and efficient centriole assembly
description	Centriole duplication is tightly regulated in vivo, but the underlying molecular mechanisms are incompletely understood. Here the authors use high-resolution structural and imaging methods to show that CEP85 directly interacts with STIL and mediates efficient centriolar targeting of STIL, PLK4 activation and centriole assembly.
format	article
author	Yi Liu Gagan D. Gupta Deepak D. Barnabas Fikret G. Agircan Shahid Mehmood Di Wu Etienne Coyaud Christopher M. Johnson Stephen H. McLaughlin Antonina Andreeva Stefan M. V. Freund Carol V. Robinson Sally W. T. Cheung Brian Raught Laurence Pelletier Mark van Breugel
author_facet	Yi Liu Gagan D. Gupta Deepak D. Barnabas Fikret G. Agircan Shahid Mehmood Di Wu Etienne Coyaud Christopher M. Johnson Stephen H. McLaughlin Antonina Andreeva Stefan M. V. Freund Carol V. Robinson Sally W. T. Cheung Brian Raught Laurence Pelletier Mark van Breugel
author_sort	Yi Liu
title	Direct binding of CEP85 to STIL ensures robust PLK4 activation and efficient centriole assembly
title_short	Direct binding of CEP85 to STIL ensures robust PLK4 activation and efficient centriole assembly
title_full	Direct binding of CEP85 to STIL ensures robust PLK4 activation and efficient centriole assembly
title_fullStr	Direct binding of CEP85 to STIL ensures robust PLK4 activation and efficient centriole assembly
title_full_unstemmed	Direct binding of CEP85 to STIL ensures robust PLK4 activation and efficient centriole assembly
title_sort	direct binding of cep85 to stil ensures robust plk4 activation and efficient centriole assembly
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/64d5bf6e3d9f4b17ae080b2ad6edfff9
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Direct binding of CEP85 to STIL ensures robust PLK4 activation and efficient centriole assembly

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