How CEP164 ciliopathy mutations impair ciliogenesis

Ciaran G. Morrison

doi:10.1016/j.str.2021.12.007

How CEP164 ciliopathy mutations impair ciliogenesis

Ciaran G. Morrison

Molecular Biosciences

Research output: Contribution to a Journal (Peer & Non Peer) › Comment/debate

2 Citations (Scopus)

Abstract

CEP164 recruits TTBK2 to the distal end of centrioles to allow primary cilium formation. In this issue of Structure, Rosa e Silva et al. (2022) present co-crystallized structures that show the molecular basis of this recruitment and define how ciliopathy mutations in CEP164 disrupt the CEP164-TTBK2 complex.

Original language	English
Pages (from-to)	4-5
Number of pages	2
Journal	Structure
Volume	30
Issue number	1
DOIs	https://doi.org/10.1016/j.str.2021.12.007
Publication status	Published - 6 Jan 2022

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10.1016/j.str.2021.12.007

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title = "How CEP164 ciliopathy mutations impair ciliogenesis",

abstract = "CEP164 recruits TTBK2 to the distal end of centrioles to allow primary cilium formation. In this issue of Structure, Rosa e Silva et al. (2022) present co-crystallized structures that show the molecular basis of this recruitment and define how ciliopathy mutations in CEP164 disrupt the CEP164-TTBK2 complex.",

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AB - CEP164 recruits TTBK2 to the distal end of centrioles to allow primary cilium formation. In this issue of Structure, Rosa e Silva et al. (2022) present co-crystallized structures that show the molecular basis of this recruitment and define how ciliopathy mutations in CEP164 disrupt the CEP164-TTBK2 complex.

UR - https://www.scopus.com/pages/publications/85123268052

U2 - 10.1016/j.str.2021.12.007

DO - 10.1016/j.str.2021.12.007

M3 - Comment/debate

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JO - Structure

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How CEP164 ciliopathy mutations impair ciliogenesis

Abstract

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