TRIP6 functions in brain ciliogenesis

Shalmali Shukla, Ronny Haenold, Pavel Urbánek, Lucien Frappart, Shamci Monajembashi, Paulius Grigaravicius, Sigrun Nagel, Woo Kee Min, Alicia Tapias, Olivier Kassel, Heike Heuer, Zhao-Qi Wang, Aspasia Ploubidou () and Peter Herrlich ()
Additional contact information
Shalmali Shukla: Leibniz Institute on Aging – Fritz Lipmann Institute (FLI)
Ronny Haenold: Leibniz Institute on Aging – Fritz Lipmann Institute (FLI)
Pavel Urbánek: Leibniz Institute on Aging – Fritz Lipmann Institute (FLI)
Lucien Frappart: Leibniz Institute on Aging – Fritz Lipmann Institute (FLI)
Shamci Monajembashi: Leibniz Institute on Aging – Fritz Lipmann Institute (FLI)
Paulius Grigaravicius: Leibniz Institute on Aging – Fritz Lipmann Institute (FLI)
Sigrun Nagel: Leibniz Institute on Aging – Fritz Lipmann Institute (FLI)
Woo Kee Min: Leibniz Institute on Aging – Fritz Lipmann Institute (FLI)
Alicia Tapias: Leibniz Institute on Aging – Fritz Lipmann Institute (FLI)
Olivier Kassel: Institute for Biological and Chemical Systems-Biological Information Processing (IBCS-BIP)
Heike Heuer: University of Duisburg-Essen
Zhao-Qi Wang: Leibniz Institute on Aging – Fritz Lipmann Institute (FLI)
Aspasia Ploubidou: Leibniz Institute on Aging – Fritz Lipmann Institute (FLI)
Peter Herrlich: Leibniz Institute on Aging – Fritz Lipmann Institute (FLI)

Nature Communications, 2021, vol. 12, issue 1, 1-16

Abstract: Abstract TRIP6, a member of the ZYXIN-family of LIM domain proteins, is a focal adhesion component. 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 localization along the axoneme, and its co-localization with other cilia components suggest a scaffold/co-transporter function for TRIP6 in cilia. Thus, this work uncovers an essential role of a LIM-domain protein assembly factor in mammalian ciliogenesis.

Date: 2021
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DOI: 10.1038/s41467-021-26057-6

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