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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; Heuer, Heike; Wang, Zhao-Qi; Ploubidou, Aspasia; Herrlich, Peter

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.


Verlagsausgabe §
DOI: 10.5445/IR/1000138976
Veröffentlicht am 14.10.2021
Cover der Publikation
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 Web of Science
Scopus
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