In:
PLOS Biology, Public Library of Science (PLoS), Vol. 20, No. 9 ( 2022-9-7), p. e3001782-
Abstract:
In metazoa, cilia assembly is a cellular process that starts with centriole to basal body maturation, migration to the cell surface, and docking to the plasma membrane. Basal body docking involves the interaction of both the distal end of the basal body and the transition fibers/distal appendages, with the plasma membrane. Mutations in numerous genes involved in basal body docking and transition zone assembly are associated with the most severe ciliopathies, highlighting the importance of these events in cilium biogenesis. In this context, the ciliate Paramecium has been widely used as a model system to study basal body and cilia assembly. However, despite the evolutionary conservation of cilia assembly events across phyla, whether the same molecular players are functionally conserved, is not fully known. Here, we demonstrated that CEP90, FOPNL, and OFD1 are evolutionary conserved proteins crucial for ciliogenesis. Using ultrastructure expansion microscopy, we unveiled that these proteins localize at the distal end of both centrioles/basal bodies in Paramecium and mammalian cells. Moreover, we found that these proteins are recruited early during centriole duplication on the external surface of the procentriole. Functional analysis performed both in Paramecium and mammalian cells demonstrate the requirement of these proteins for distal appendage assembly and basal body docking. Finally, we show that mammalian centrioles require another component, Moonraker (MNR), to recruit OFD1, FOPNL, and CEP90, which will then recruit the distal appendage proteins CEP83, CEP89, and CEP164. Altogether, we propose that this OFD1, FOPNL, and CEP90 functional module is required to determine in mammalian cells the future position of distal appendage proteins.
Type of Medium:
Online Resource
ISSN:
1545-7885
DOI:
10.1371/journal.pbio.3001782
DOI:
10.1371/journal.pbio.3001782.g001
DOI:
10.1371/journal.pbio.3001782.g002
DOI:
10.1371/journal.pbio.3001782.g003
DOI:
10.1371/journal.pbio.3001782.g004
DOI:
10.1371/journal.pbio.3001782.g005
DOI:
10.1371/journal.pbio.3001782.g006
DOI:
10.1371/journal.pbio.3001782.g007
DOI:
10.1371/journal.pbio.3001782.g008
DOI:
10.1371/journal.pbio.3001782.g009
DOI:
10.1371/journal.pbio.3001782.s001
DOI:
10.1371/journal.pbio.3001782.s002
DOI:
10.1371/journal.pbio.3001782.s003
DOI:
10.1371/journal.pbio.3001782.s004
DOI:
10.1371/journal.pbio.3001782.s005
DOI:
10.1371/journal.pbio.3001782.s006
DOI:
10.1371/journal.pbio.3001782.s007
DOI:
10.1371/journal.pbio.3001782.s008
DOI:
10.1371/journal.pbio.3001782.s009
DOI:
10.1371/journal.pbio.3001782.s010
DOI:
10.1371/journal.pbio.3001782.s011
DOI:
10.1371/journal.pbio.3001782.s012
DOI:
10.1371/journal.pbio.3001782.s013
DOI:
10.1371/journal.pbio.3001782.s014
DOI:
10.1371/journal.pbio.3001782.s015
DOI:
10.1371/journal.pbio.3001782.s016
DOI:
10.1371/journal.pbio.3001782.s017
DOI:
10.1371/journal.pbio.3001782.s018
DOI:
10.1371/journal.pbio.3001782.s019
DOI:
10.1371/journal.pbio.3001782.s020
DOI:
10.1371/journal.pbio.3001782.s021
DOI:
10.1371/journal.pbio.3001782.s022
DOI:
10.1371/journal.pbio.3001782.s023
DOI:
10.1371/journal.pbio.3001782.s024
Language:
English
Publisher:
Public Library of Science (PLoS)
Publication Date:
2022
detail.hit.zdb_id:
2126773-X
Bookmarklink