scholarly journals EFA6A, an exchange factor for Arf6, regulates early steps in ciliogenesis

2021 ◽  
Vol 134 (2) ◽  
pp. jcs249565
Author(s):  
Mariagrazia Partisani ◽  
Carole L. Baron ◽  
Rania Ghossoub ◽  
Racha Fayad ◽  
Sophie Pagnotta ◽  
...  

ABSTRACTCiliogenesis is a coordinated process initiated by the recruitment and fusion of pre-ciliary vesicles at the distal appendages of the mother centriole through mechanisms that remain unclear. Here, we report that EFA6A (also known as PSD), an exchange factor for the small G protein Arf6, is involved in early stage of ciliogenesis by promoting the fusion of distal appendage vesicles forming the ciliary vesicle. EFA6A is present in the vicinity of the mother centriole before primary cilium assembly and prior to the arrival of Arl13B-containing vesicles. During ciliogenesis, EFA6A initially accumulates at the mother centriole and later colocalizes with Arl13B along the ciliary membrane. EFA6A depletion leads to the inhibition of ciliogenesis, the absence of centrosomal Rab8-positive structures and the accumulation of Arl13B-positive vesicles around the distal appendages. Our results uncover a novel fusion machinery, comprising EFA6A, Arf6 and Arl13B, that controls the coordinated fusion of ciliary vesicles docked at the distal appendages of the mother centriole.

2013 ◽  
Vol 24 (4) ◽  
pp. 453-464 ◽  
Author(s):  
Johanna R. Schaub ◽  
Tim Stearns

The primary cilium is a microtubule-based structure found in most cell types in mammals. Disruption of cilium function causes a diverse set of human diseases collectively known as ciliopathies. We report that Rab effector–related proteins Rab-interacting lysosomal protein-like 1 (Rilpl1) and Rilpl2 regulate protein localization in the primary cilium. Rilpl2 was initially identified as up-regulated in ciliating mouse tracheal epithelial cells. Rilpl1 and Rilpl2 both localize to the primary cilium and centrosome, Rilpl1 specifically to the distal end of the mother centriole. Live-cell microscopy reveals that Rilpl2 primary cilium localization is dynamic and that it is associated with tubulovesicular structures at the base of the cilium. Depletion of Rilpl1 and Rilpl2 results in accumulation of signaling proteins in the ciliary membrane and prevents proper epithelial cell organization in three-dimensional culture. These data suggest that Rilp-like proteins function in regulation of ciliary membrane protein concentration by promoting protein removal from the primary cilium.


2010 ◽  
Vol 3 (1) ◽  
Author(s):  
Alexey V Karpushev ◽  
Daria V Ilatovskaya ◽  
Alexander Staruschenko

2014 ◽  
Vol 106 (2) ◽  
pp. 614a
Author(s):  
Seigo Iwata ◽  
Shinsaku Maruta

2002 ◽  
Vol 291 (4) ◽  
pp. 744-750 ◽  
Author(s):  
Fatima Lekmine ◽  
Antonella Sassano ◽  
Shahab Uddin ◽  
Beata Majchrzak ◽  
Osamu Miura ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document