
@article {147286,
	title = {Localisation and function of key axonemal microtubule inner proteins and dynein docking complex members reveal extensive diversity among vertebrate motile cilia.},
	journal = {Development},
	volume = {151},
	year = {2024},
	month = {2024 Jul 15},
	abstract = {<p>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.</p>
},
	keywords = {Animals, Axonemal Dyneins, Axoneme, Cilia, Dyneins, Mice, Microtubule-Associated Proteins, Microtubules, Zebrafish, Zebrafish Proteins},
	issn = {1477-9129},
	doi = {10.1242/dev.202737},
	author = {Lu, Hao and Twan, Wang Kyaw and Ikawa, Yayoi and Khare, Vani and Mukherjee, Ishita and Schou, Kenneth B{\o}dtker and Chua, Kai Xin and Aqasha, Adam and Chakrabarti, Saikat and Hamada, Hiroshi and Roy, Sudipto}
}
