TRIP6 functions in brain ciliogenesis
Shukla, Shalmali; Haenold, Ronny; Urbánek, Pavel; Frappart, Lucien; Monajembashi, Shamci; Grigaravicius, Paulius; Nagel, Sigrun; Min, Woo Kee; Tapias, Alicia; Kassel, Olivier
1; Heuer, Heike; Wang, Zhao-Qi; Ploubidou, Aspasia; Herrlich, Peter
1 Karlsruher Institut für Technologie (KIT)
1; Heuer, Heike; Wang, Zhao-Qi; Ploubidou, Aspasia; Herrlich, Peter1 Karlsruher Institut für Technologie (KIT)
Abstract (englisch):
TRIP6, a member of the ZYXIN-family of LIM domain proteins, is a focal adhesion compo-
nent. Trip6 deletion in the mouse, reported here, reveals a function in the brain: ependymal
and choroid plexus epithelial cells are carrying, unexpectedly, fewer and shorter cilia, are
poorly differentiated, and the mice develop hydrocephalus. TRIP6 carries numerous protein
interaction domains and its functions require homodimerization. Indeed, TRIP6 disruption
in vitro (in a choroid plexus epithelial cell line), via RNAi or inhibition of its homodimerization,
confirms its function in ciliogenesis. Using super-resolution microscopy, we demonstrate
TRIP6 localization at the pericentriolar material and along the ciliary axoneme. The
requirement for homodimerization which doubles its interaction sites, its punctate localiza-
tion along the axoneme, and its co-localization with other cilia components suggest a scaf-
fold/co-transporter function for TRIP6 in cilia. Thus, this work uncovers an essential role of a
LIM-domain protein assembly factor in mammalian ciliogenesis.
nent. Trip6 deletion in the mouse, reported here, reveals a function in the brain: ependymal
and choroid plexus epithelial cells are carrying, unexpectedly, fewer and shorter cilia, are
poorly differentiated, and the mice develop hydrocephalus. TRIP6 carries numerous protein
interaction domains and its functions require homodimerization. Indeed, TRIP6 disruption
in vitro (in a choroid plexus epithelial cell line), via RNAi or inhibition of its homodimerization,
confirms its function in ciliogenesis. Using super-resolution microscopy, we demonstrate
TRIP6 localization at the pericentriolar material and along the ciliary axoneme. The
requirement for homodimerization which doubles its interaction sites, its punctate localiza-
tion along the axoneme, and its co-localization with other cilia components suggest a scaf-
fold/co-transporter function for TRIP6 in cilia. Thus, this work uncovers an essential role of a
LIM-domain protein assembly factor in mammalian ciliogenesis.
| Zugehörige Institution(en) am KIT | Institut für Biologische und Chemische Systeme (IBCS) |
| Publikationstyp | Zeitschriftenaufsatz |
| Publikationsmonat/-jahr | 12.2021 |
| Sprache | Englisch |
| Identifikator | ISSN: 2041-1723 KITopen-ID: 1000138976 |
| HGF-Programm | 47.14.02 (POF IV, LK 01) Information Storage and Processing in the Cell Nucleus |
| Erschienen in | Nature Communications |
| Verlag | Nature Research |
| Band | 12 |
| Heft | 1 |
| Seiten | Art.-Nr.: 5887 |
| Vorab online veröffentlicht am | 07.10.2021 |
| Nachgewiesen in | Scopus Dimensions Web of Science |