Abstract:

Cilia are cell-surface organelles crucial for various signal transduction pathways and the spatial distribution of proteins within cilia is dynamically regulated by the intraflagellar transport (IFT) machinery. K63-linked polyubiquitination has been linked to the IFT-mediated retrieval of proteins from cilia, however, the mechanisms by which polyubiquitinated proteins are recognized for export remain unclear. Here, I present my work identifying that CFAP36, a highly conserved ciliary protein of previously unknown function, binds polyubiquitinated proteins and links them specifically to retrograde IFT trains. In addition, ARL3, a small GTPase known primarily for its role as a cargo displacement factor, functions as a cargo loading factor for retrograde transport, enhancing the binding of polyubiquitinated cargos by CFAP36

Bio:

Following training in structural biology at the Max-Planck institute in Dortmund, Germany, Sven obtained his Ph.D. with Sir Philip Cohen at the MRC PPU in 2020, where he worked on the allosteric regulation of protein kinases through pseudokinases. Next, during postdoctoral training with Yogesh Kulathu, also at the MRC PPU, he worked on branched ubiquitin chains and deubiquitinases. In 2022, Sven joined the Brown lab at Harvard Medical School to investigate how ubiquitinated proteins are retrieved from cilia, for which he was awarded a Sara Elizabeth O'Brien Trust Postdoc Fellowship in 2023. Outside the lab, Sven applies his biochemistry skills to working with yeast for brewing and bread baking, and enjoys hiking in the New England mountains.