Adrian Pascal Nievergelt

Abstract Cilia assembly and function rely on the bidirectional transport of components between the cell body and ciliary tip via Intraflagellar Transport (IFT) trains. Anterograde and retrograde IFT trains travel along the B- and A-tubules of microtubule doublets, respectively, ensuring smooth traffic flow. However, the mechanism underlying this segregation remains unclear.

Abstract The glycocalyx, a highly heterogeneous glycoprotein layer of cilia regulates adhesion and force transduction, and is involved in signalling. The high-resolution molecular architecture of this layer is currently not understood. We describe the structure of the ciliary coat in the green alga Chlamydomonas reinhardtii by cryo-electron tomography and proteomic approaches and present the high-resolution cryoEM structure of the main component, FMG1B.

Abstract The outermost layer of cilia is a coat of membrane anchored, glycosylated proteins often referred to as glycocalyx. This highly heterogeneous layer provides functions from regulation of adhesion, force transduction and protection to signalling. Despite its importance, there is a lack of studies focusing on the high-resolution molecular architecture of this layer.