Open AccessCentrosomal protein Dzip1l binds Cby, promotes ciliary bud formation, and acts redundantly with Bromi to regulate ciliogenesis in the mouse
Author(s) -
Chengbing Wang,
Jia Li,
KenIchi Takemaru,
Xiaogang Jiang,
Guoqiang Xu,
Baolin Wang
Publication year - 2018
Publication title -
development
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.754
H-Index - 325
eISSN - 1477-9129
pISSN - 0950-1991
DOI - 10.1242/dev.164236
Subject(s) - ciliogenesis , biology , cilium , microbiology and biotechnology , basal body , axoneme , centriole , smoothened , intraflagellar transport , ciliopathy , hedgehog signaling pathway , microtubule , mutant , signal transduction , flagellum , genetics , phenotype , gene
The primary cilium is a microtubule-based organelle required for Hedgehog (Hh) signaling and consists of basal body, ciliary axoneme, and transition zone, a compartment between the first two structures. The transition zone serves as a gatekeeper to control protein composition in cilia, but less is known about its role in ciliary bud formation. Here, we show that centrosomal protein Dzip1l is required for Hh signaling between Smoothened and Sufu. Dzip1l colocalizes with basal body appendage proteins and Rpgrip1l, a transition zone protein. Loss of Dzip1l results in reduced ciliogenesis and dysmorphic cilia in vivo. Dzip1l interacts with and acts upstream of Cby, an appendage protein, in ciliogenesis. Dzip1l also has overlapping functions with Bromi in ciliogenesis, cilia morphogenesis, and neural tube patterning. Loss of Dzip1l arrests ciliogenesis at the stage of ciliary bud formation from the transition zone. Consistent with this, Dzip1l mutant cells fail to remove the capping protein Cp110 from the distal end of mother centrioles and recruit Rpgrip1l to the transition zone. Therefore, Dzip1l promotes ciliary bud formation and is required for the integrity of transition zone.