Dr. Mateusz Czub
5232 Villigen PSI
Mateusz Czub completed his undergraduate studies at the Jagiellonian University (Krakow, Poland) where he attained a B.Sc. in 2015 and M.Sc. degree in 2017 majoring in Chemistry. In 2016 he joined the group of Prof. Wladek Minor at the University of Virginia (Virginia, USA), in the framework of the Visiting Research Graduate Traineeship Program, where he completed his Master’s project. In 2017 Mateusz started Ph.D. Program in Biomedical Sciences at the University of Virginia, continuing his work in the group of Prof. Wladek Minor (Department of Molecular Physiology and Biological Physics). His area of research during the Ph.D. studies was focused on the interactions of serum albumin, the most abundant protein in mammalian blood plasma, with different classes of FDA-approved drugs and metabolites. Mateusz used structural and biophysical methods to characterize these interactions at the molecular level. For his work, he was awarded the Robert R. Wagner Fellowship. Mateusz obtained his Ph.D. in Biophysics in December 2020. In January 2021, he joined the group of Prof. Michel Steinmetz in the Laboratory of Biomolecular Research (LBR). Currently, Mateusz is a Marie Sklodowska-Curie Postdoctoral Fellow under the 3i scheme at the Paul Scherrer Institute (Villigen, Switzerland).
Mateusz's current research focuses on microtubule plus-end tracking proteins (+TIPs). +TIPs localize to and track dynamic microtubule plus ends where they form complex protein networks, which are implicated in virtually all microtubule-based processes. For instance, the Kar9-mediated +TIP network in budding yeast drives nuclear positioning during mitosis and cell mating in an actin filament/myosin-dependent manner. Protein members of the Kar9 network have recently been observed to undergo liquid-liquid phase separation in vitro, but their physicochemical properties, organization, and regulation are poorly understood. In his project, conducted in the group of Prof. Michel Steinmetz, Mateusz investigates the structural, biochemical, and material properties of the Kar9 network and tests a hypothesis that specialized +TIP networks are organized as phase-separated bodies around dynamic microtubule ends. Mateusz believes that the results that will be obtained in this project will contribute to our understanding of the fundamental principles driving the assembly and function of phase-separated protein networks in cells, and how this can contribute to mechanical force coupling.
Kar9-mediated +TIP network in budding yeast was hypothesized to be organized as phase-separated bodies around dynamic microtubule ends. The formation of a phase-separated protein droplet around microtubule plus-ends could “glue” them to their cargoes like the mitotic spindle.