Cep164 mediates vesicular docking to the mother centriole during early steps of ciliogenesis

Cilia formation is a multi-step process that starts with the docking of a vesicle at the distal part of the mother centriole. This step marks the conversion of the mother centriole into the basal body, from which axonemal microtubules extend to form the ciliary compartment. How vesicles are stably a...

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Bibliographic Details
Main Authors: Schmidt, Kerstin Natascha (Author) , Neuner, Annett (Author) , Pereira, Gislene (Author)
Format: Article (Journal)
Language:English
Published: December 17, 2012
In: The journal of cell biology
Year: 2012, Volume: 199, Issue: 7, Pages: 1083-1101
ISSN:1540-8140
DOI:10.1083/jcb.201202126
Online Access:Verlag, kostenfrei, Volltext: http://dx.doi.org/10.1083/jcb.201202126
Verlag, kostenfrei, Volltext: http://jcb.rupress.org/content/199/7/1083
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Author Notes:Kerstin N. Schmidt, Stefanie Kuhns, Annett Neuner, Birgit Hub, Hanswalter Zentgraf, and Gislene Pereira
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Summary:Cilia formation is a multi-step process that starts with the docking of a vesicle at the distal part of the mother centriole. This step marks the conversion of the mother centriole into the basal body, from which axonemal microtubules extend to form the ciliary compartment. How vesicles are stably attached to the mother centriole to initiate ciliary membrane biogenesis is unknown. Here, we investigate the molecular role of the mother centriolar component Cep164 in ciliogenesis. We show that Cep164 was indispensable for the docking of vesicles at the mother centriole. Using biochemical and functional assays, we identified the components of the vesicular transport machinery, the GEF Rabin8 and the GTPase Rab8, as interacting partners of Cep164. We propose that Cep164 is targeted to the apical domain of the mother centriole to provide the molecular link between the mother centriole and the membrane biogenesis machinery that initiates cilia formation.
Item Description:Gesehen am 11.05.2017
Physical Description:Online Resource
ISSN:1540-8140
DOI:10.1083/jcb.201202126