Link to bioRxiv paper:
http://biorxiv.org/cgi/content/short/2023.07.24.550339v1?rss=1

Authors: Shaughnessy, R., Serres, M., Escot, S., Hammich, H., Cuvelier, F., Salles, A., Rocancourt, M., Verdon, Q., Gaffuri, A.-L., Sourigues, Y., Malherbe, G., Velikovsky, L., Chardon, F., Tinevez, J.-Y., Callebaut, I., Formstecher, E., Houdusse, A., David, N., Pylypenko, O., Echard, A.

Abstract:
Cilia protrude from the cell surface and play critical roles in intracellular signaling, environmental sensing and development. Actin-dependent contractility and intracellular trafficking are both required for ciliogenesis, but little is known about how these processes are coordinated. Here, we identified a Rac1- and Rab35-binding protein with a truncated BAR domain that we named MiniBAR (aka KIAA0355/GARRE) which plays a key role in ciliogenesis. MiniBAR colocalizes with Rac1 and Rab35 at the plasma membrane and on intracellular vesicles trafficking to the ciliary base and exhibits remarkable fast pulses at the ciliary membrane. MiniBAR depletion leads to short cilia resulting from abnormal Rac-GTP/Rho-GTP levels, increased acto-myosin-II-dependent contractility together with defective trafficking of IFT88 and ARL13B into cilia. MiniBAR-depleted zebrafish embryos display dysfunctional short cilia and hallmarks of ciliopathies including left-right asymmetry defects. Thus, MiniBAR is a unique dual Rac and Rab effector that controls both actin cytoskeleton and membrane trafficking for ciliogenesis.

Copy rights belong to original authors. Visit the link for more info

Podcast created by Paper Player, LLC