Vesicular trafficking plays a role in centriole disengagement and duplication
Reinecke, James B
Nichols, Benjamin J
McLamarrah, Tiffany A
Rogers, Gregory C
AffiliationUniv Arizona, Canc Ctr, Dept Cellular & Mol Med
MetadataShow full item record
PublisherAMER SOC CELL BIOLOGY
CitationXie, S., Reinecke, J. B., Farmer, T., Bahl, K., Yeow, I., Nichols, B. J., ... & Caplan, S. (2018). Vesicular trafficking plays a role in centriole disengagement and duplication. Molecular biology of the cell, 29(22), 2622-2631.
JournalMOLECULAR BIOLOGY OF THE CELL
Rights© 2018 Xie, Reinecke, et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License.
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AbstractCentrosomes are the major microtubule-nucleating and microtubule-organizing centers of cells and play crucial roles in microtubule anchoring, organelle positioning, and ciliogenesis. At the centrosome core lies a tightly associated or "engaged" mother-daughter centriole pair. During mitotic exit, removal of centrosomal proteins pericentrin and Cep215 promotes "disengagement" by the dissolution of intercentriolar linkers, ensuring a single centriole duplication event per cell cycle. Herein, we explore a new mechanism involving vesicular trafficking for the removal of centrosomal Cep215. Using small interfering RNA and CRISPR/ Cas9 gene-edited cells, we show that the endocytic protein EHD1 regulates Cep215 transport from centrosomes to the spindle midbody, thus facilitating disengagement and duplication. We demonstrate that EHD1 and Cep215 interact and show that Cep215 displays increased localization to vesicles containing EHD1 during mitosis. Moreover, Cep215-containing vesicles are positive for internalized transferrin, demonstrating their endocytic origin. Thus, we describe a novel relationship between endocytic trafficking and the centrosome cycle, whereby vesicles of endocytic origin are used to remove key regulatory proteins from centrosomes to control centriole duplication.
VersionFinal published version
SponsorsNational Institute of General Medical Sciences (NIGMS) [R01GM074876, P30GM106397]; National Cancer Institute [P30 CA23074]; NIH/NIGMS [R01GFM110166, R01GM126035]