Degradation of Cep68 and PCNT cleavage mediate Cep215 removal from the PCM to allow centriole separation, disengagement and licensing.
Degradation of Cep68 and PCNT cleavage mediate Cep215 removal from the PCM to allow centriole separation, disengagement and licensing.
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DOI：
10.1038/ncb3076
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发表时间：
2015-01
影响因子：
21.3
通讯作者：
中科院分区：
文献类型：
--
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An intercentrosomal linker keeps the cell’s two centrosomes joined together until it is dissolved at the onset of mitosis. A second connection keeps daughter centrioles engaged to their mothers until they lose their orthogonal arrangement at the end of mitosis. Centriole disengagement is required to license centrioles for duplication. We show that the intercentrosomal linker protein Cep68 is degraded in prometaphase through the SCFβTrCP (Skp1-Cul1-F-box protein) ubiquitin ligase complex. Cep68 degradation is initiated by PLK1 phosphorylation of Cep68 on Ser332, allowing recognition by βTrCP. We also found that Cep68 forms a complex with Cep215/Cdk5Rap2 and PCNT/Pericentrin, two PCM (pericentriolar material) proteins involved in centriole engagement. Cep68 requires two different pools of Cep215. We propose that Cep68 degradation allows Cep215 removal from the peripheral PCM preventing centriole separation following disengagement, whereas PCNT cleavage mediates Cep215 removal from the core of the PCM to inhibit centriole disengagement and duplication.
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影响因子：
4
作者：
Guderian, Gernot;Westendorf, Jens;Nigg, Erich A.
通讯作者：
Nigg, Erich A.
影响因子：
21.3
作者：
Lawo, Steffen;Hasegan, Monica;Pelletier, Laurence
通讯作者：
Pelletier, Laurence
Cdk5rap2 与 Pericentrin 相互作用以维持发育中神经皮层的神经祖细胞库
影响因子：
16.2
作者：
Buchman, Joshua J.;Tseng, Huan-Chung;Tsai, Li-Huei
通讯作者：
Tsai, Li-Huei
影响因子：
9.2
作者：
Cabral, Gabriela;Sans, Sabina Sanegre;Cowan, Carrie R.;Dammermann, Alexander
通讯作者：
Dammermann, Alexander
DOI：
10.1083/jcb.200504107
发表时间：
2005-10-10
期刊：
The Journal of cell biology
影响因子：
--
作者：
Bahe S;Stierhof YD;Wilkinson CJ;Leiss F;Nigg EA
通讯作者：
Nigg EA