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XB-ART-58620
J Cell Biol January 3, 2022; 221 (1):
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CEP97 phosphorylation by Dyrk1a is critical for centriole separation during multiciliogenesis.

Lee M , Nagashima K , Yoon J , Sun J , Wang Z , Carpenter C , Lee HK , Hwang YS , Westlake CJ , Daar IO .


Abstract
Proper cilia formation in multiciliated cells (MCCs) is necessary for appropriate embryonic development and homeostasis. Multicilia share many structural characteristics with monocilia and primary cilia, but there are still significant gaps in our understanding of the regulation of multiciliogenesis. Using the Xenopus embryo, we show that CEP97, which is known as a negative regulator of primary cilia formation, interacts with dual specificity tyrosine phosphorylation regulated kinase 1A (Dyrk1a) to modulate multiciliogenesis. We show that Dyrk1a phosphorylates CEP97, which in turn promotes the recruitment of Polo-like kinase 1 (Plk1), which is a critical regulator of MCC maturation that functions to enhance centriole disengagement in cooperation with the enzyme Separase. Knockdown of either CEP97 or Dyrk1a disrupts cilia formation and centriole disengagement in MCCs, but this defect is rescued by overexpression of Separase. Thus, our study reveals that Dyrk1a and CEP97 coordinate with Plk1 to promote Separase function to properly form multicilia in vertebrate MCCs.

PubMed ID: 34787650
Article link: J Cell Biol
Grant support: [+]

Species referenced: Xenopus laevis
Genes referenced: ccdc78 cdc20b cep97 deup1 dyrk1a.2 isyna1 mcc plk1
GO keywords: centriole assembly
Antibodies: Actb Ab9 Cep97 Ab1 Dyrk1a Ab1 Gapdh Ab3
Morpholinos: cep97 MO1 dyrk1a MO2


Article Images: [+] show captions
References [+] :
Al Jord, Calibrated mitotic oscillator drives motile ciliogenesis. 2018, Pubmed