Author response: STIL binding to Polo-box 3 of PLK4 regulates centriole duplication

Arquint, Christian; Gabryjonczyk, Anna-Maria; Imseng, Stefan; Böhm, Raphael; Sauer, Evelyn; Hiller, Sebastian; Nigg, Erich A.; Maier, Timm

doi:10.7554/elife.07888.022

Cited by 2 publications

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Bimodal Binding of STIL to Plk4 Controls Proper Centriole Copy Number

et al. 2018

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The number of centrioles is tightly controlled to ensure bipolar spindle assembly, which is a prerequisite to maintain genome integrity. However, our understanding of the fundamental principle that governs the formation of a single procentriole per parental centriole is incomplete. Here, we show that the local restriction of Plk4, a master regulator of the procentriole formation, is achieved by a bimodal interaction of STIL with Plk4. We demonstrate that the conserved short coiled-coil region of STIL binds to and protects Plk4 from protein degradation at the site of procentriole formation. On the other hand, the conserved C-terminal region of STIL named truncated in microcephaly (TIM) domain promotes autophosphorylation and degradation of adjacent Plk4 by the direct interaction. Thus, we propose that positive and negative regulation based on the bimodal binding of Plk4 and STIL ensures the formation of a single procentriole per parental centriole.

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Bimodal Binding of STIL to Plk4 Controls Proper Centriole Copy Number

et al. 2018

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Cep57 and Cep57l1 cooperate to recruit the Cep63-Cep152 complex for centriole biogenesis

Zhao

Yang

Duan

et al. 2019

Preprint

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Cep152 and Cep63 act as the cradle and recruit Plk4 to initiate the centriole biogenesis in a mother centriole dependent manner. However, how the Cep152-Cep63 complex is targeted to the proximal end of mother centrioles is unclear. In this study, we show that Cep57 and its paralog, Cep57l1, colocalize with Cep63 and Cep152 at the proximal end of mother centrioles in both cycling cells and differentiated multiciliated cells. Both Cep57 and Cep57l1 associate with the Cep152-Cep63 complex by directly binding to the centrosomal targeting region of Cep63. Co-depletion of Cep57 and Cep57l1 blocks the loading of Cep63-Cep152 to the centriole and subsequently prevents centriole duplication. We propose that Cep57 and Cep57l1 act together to ensure the recruitment of the Cep63-Cep152 complex to the mother centrioles for procentriole formation. Summary statement Cep57 and its paralog, Cep57l1, cooperatively act as a molecular scaffold to recruit the Cep63-Cep152 cradle to the proximal end of centrioles in the early stages of centriole duplication.

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Author response: STIL binding to Polo-box 3 of PLK4 regulates centriole duplication

Cited by 2 publications

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Bimodal Binding of STIL to Plk4 Controls Proper Centriole Copy Number

Bimodal Binding of STIL to Plk4 Controls Proper Centriole Copy Number

Cep57 and Cep57l1 cooperate to recruit the Cep63-Cep152 complex for centriole biogenesis

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