PUBLICATION
Localisation and function of key axonemal microtubule inner proteins and dynein docking complex members reveal extensive diversity among vertebrate motile cilia
- Authors
- Lu, H., Twan, W.K., Ikawa, Y., Khare, V., Mukherjee, I., Schou, K.B., Chua, K.X., Aqasha, A., Chakrabarti, S., Hamada, H., Roy, S.
- ID
- ZDB-PUB-240716-2
- Date
- 2024
- Source
- Development (Cambridge, England) 151(14): (Journal)
- Registered Authors
- Roy, Sudipto
- Keywords
- (9+0) cilia, (9+2) cilia, Axoneme, CFAP53, Centriolar satellites, LRQ motif, Left-right organiser, MNS1, Microtubule inner protein, Mouse, Outer dynein arm docking complex, Zebrafish
- MeSH Terms
-
- Animals
- Axonemal Dyneins/genetics
- Axonemal Dyneins/metabolism
- Axoneme*/metabolism
- Axoneme*/ultrastructure
- Cilia*/metabolism
- Cilia*/ultrastructure
- Dyneins/metabolism
- Mice
- Microtubule-Associated Proteins/genetics
- Microtubule-Associated Proteins/metabolism
- Microtubules/metabolism
- Zebrafish*/metabolism
- Zebrafish Proteins/genetics
- Zebrafish Proteins/metabolism
- PubMed
- 39007638 Full text @ Development
Citation
Lu, H., Twan, W.K., Ikawa, Y., Khare, V., Mukherjee, I., Schou, K.B., Chua, K.X., Aqasha, A., Chakrabarti, S., Hamada, H., Roy, S. (2024) Localisation and function of key axonemal microtubule inner proteins and dynein docking complex members reveal extensive diversity among vertebrate motile cilia. Development (Cambridge, England). 151(14):.
Abstract
Vertebrate motile cilia are classified as (9+2) or (9+0), based on the presence or absence of the central pair apparatus, respectively. Cryogenic electron microscopy analyses of (9+2) cilia have uncovered an elaborate axonemal protein composition. The extent to which these features are conserved in (9+0) cilia remains unclear. CFAP53, a key axonemal filamentous microtubule inner protein (fMIP) and a centriolar satellites component, is essential for motility of (9+0), but not (9+2) cilia. Here, we show that in (9+2) cilia, CFAP53 functions redundantly with a paralogous fMIP, MNS1. MNS1 localises to ciliary axonemes, and combined loss of both proteins in zebrafish and mice caused severe outer dynein arm loss from (9+2) cilia, significantly affecting their motility. Using immunoprecipitation, we demonstrate that, whereas MNS1 can associate with itself and CFAP53, CFAP53 is unable to self-associate. We also show that additional axonemal dynein-interacting proteins, two outer dynein arm docking (ODAD) complex members, show differential localisation between types of motile cilia. Together, our findings clarify how paralogous fMIPs, CFAP53 and MNS1, function in regulating (9+2) versus (9+0) cilia motility, and further emphasise extensive structural diversity among these organelles.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping