Cep43, also known as centrosomal protein 43, plays a crucial role in cilia-related processes. Cilia are important organelles for signaling and locomotion in eukaryotic cells, and Cep43 is involved in the assembly of IFT complexes into IFT trains for ciliary entry. It functions through specific domain-mediated interactions within the ciliary base complex [1].

Structural modeling suggests that the N-terminal domain of Cep43 forms a homo-dimer. This dimer anchors at the subdistal appendages of cilia by directly interacting with CEP350. A long linker separates this N-terminal domain from the C-terminal domain, which captures CEP19 above the subdistal appendages and near the distal appendages. These interactions are vital for the proper architecture of RabL2-associated complexes at the ciliary base, and thus for ciliary entry [1].

In conclusion, Cep43 is essential for the structural organization of ciliary complexes, specifically in the process of IFT train assembly and ciliary entry. Understanding the function of Cep43 through structural modeling provides insights into ciliary-related biological processes. Although no KO/CKO mouse models were mentioned in the provided references, the findings highlight its importance in ciliary function and potentially related diseases where ciliary function is disrupted [1].

References:

1. Boegholm, Niels, Petriman, Narcis A, Tanvir, Niaj M, Lorentzen, Esben. 2024. Architecture of RabL2-associated complexes at the ciliary base: A structural modeling perspective: Deciphering the structural organization of ciliary RabL2 complexes. In BioEssays : news and reviews in molecular, cellular and developmental biology, 46, e2300222. doi:10.1002/bies.202300222. https://pubmed.ncbi.nlm.nih.gov/38991980/