A novel Cep120-dependent mechanism inhibits centriole maturation in quiescent cells.

Abstract:

:The two centrioles of the centrosome in quiescent cells are inherently asymmetric structures that differ in age, morphology and function. How these asymmetric properties are established and maintained during quiescence remains unknown. Here, we show that a daughter centriole-associated ciliopathy protein, Cep120, plays a critical inhibitory role at daughter centrioles. Depletion of Cep120 in quiescent mouse and human cells causes accumulation of pericentriolar material (PCM) components including pericentrin, Cdk5Rap2, ninein and Cep170. The elevated PCM levels result in increased microtubule-nucleation activity at the centrosome. Consequently, loss of Cep120 leads to aberrant dynein-dependent trafficking of centrosomal proteins, dispersal of centriolar satellites, and defective ciliary assembly and signaling. Our results indicate that Cep120 helps to maintain centrosome homeostasis by inhibiting untimely maturation of the daughter centriole, and defines a potentially new molecular defect underlying the pathogenesis of ciliopathies such as Jeune Asphyxiating Thoracic Dystrophy and Joubert syndrome.

journal_name

Elife

journal_title

eLife

authors

Betleja E,Nanjundappa R,Cheng T,Mahjoub MR

doi

10.7554/eLife.35439

subject

Has Abstract

pub_date

2018-05-09 00:00:00

issn

2050-084X

pii

35439

journal_volume

7

pub_type

杂志文章

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