EMD-20162

Subtomogram averaging
22.0 Å
EMD-20162 Deposition: 26/04/2019
Map released: 13/11/2019
Last modified: 12/08/2020
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-20162

The central pair apparatus focusing on the C1a-e-c supercomplex extracted from the cryo-electron tomography and subtomographic average of isolated Chlamydomonas fap76-1 mutant axoneme

EMD-20162

Subtomogram averaging
22.0 Å
EMD-20162 Deposition: 26/04/2019
Map released: 13/11/2019
Last modified: 12/08/2020
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Chlamydomonas reinhardtii
Sample: The C1a-e-c supercomplex of central pair apparatus averaged from Chlamydomonas fap76-1 mutant cilia

Deposition Authors: Fu G, Nicastro D
Structural organization of the C1a-e-c supercomplex within the ciliary central apparatus.
Fu G , Zhao L, Dymek E, Hou Y , Song K, Phan N, Shang Z, Smith EF, Witman GB , Nicastro D
(2019) J. Cell Biol. , 218 , 4236 - 4251
PUBMED: 31672705
DOI: doi:10.1083/jcb.201906006
ISSN: 1540-8140
ASTM: JCLBA3
Abstract:
Nearly all motile cilia contain a central apparatus (CA) composed of two connected singlet microtubules with attached projections that play crucial roles in regulating ciliary motility. Defects in CA assembly usually result in motility-impaired or paralyzed cilia, which in humans causes disease. Despite their importance, the protein composition and functions of the CA projections are largely unknown. Here, we integrated biochemical and genetic approaches with cryo-electron tomography to compare the CA of wild-type Chlamydomonas with CA mutants. We identified a large (>2 MD) complex, the C1a-e-c supercomplex, that requires the PF16 protein for assembly and contains the CA components FAP76, FAP81, FAP92, and FAP216. We localized these subunits within the supercomplex using nanogold labeling and show that loss of any one of them results in impaired ciliary motility. These data provide insight into the subunit organization and 3D structure of the CA, which is a prerequisite for understanding the molecular mechanisms by which the CA regulates ciliary beating.