A5023113725- Ubiquitin and proteasome pathways
- Sphingolipid Metabolism and Signaling
- Cancer-related Molecular Pathways
- Protein Degradation and Inhibitors
- Lipid Membrane Structure and Behavior
- Endoplasmic Reticulum Stress and Disease
- Genetics and Neurodevelopmental Disorders
- Nuclear Structure and Function
- Peptidase Inhibition and Analysis
- ATP Synthase and ATPases Research
- Erythrocyte Function and Pathophysiology
- Cellular transport and secretion
- Glycosylation and Glycoproteins Research
Research Institute of Molecular Pathology
2021-2024
Medical University of Vienna
2022-2023
Vienna Biocenter
2022-2023
Heidelberg University
2016-2019
UBR5 is a nuclear E3 ligase that ubiquitinates vast range of substrates for proteasomal degradation. This HECT domain-containing ubiquitin has recently been identified as an important regulator oncogenes, e.g., MYC, but little known about its structure or mechanisms substrate engagement and ubiquitination. Here, we present the cryo-EM human UBR5, revealing α-solenoid scaffold with numerous protein-protein interacting motifs, assembled into antiparallel dimer adopts further oligomeric states....
Cell membranes contain hundreds to thousands of individual lipid species that are structural importance but also specifically interact with proteins. Due their highly controlled synthesis and role in signaling events sphingolipids an intensely studied class lipids. In order investigate metabolism study proteins interacting sphingolipids, metabolic labeling based on photoactivatable sphingoid bases is the most straightforward approach. monitor protein-lipid-crosslink products, sphingosine...
ABSTRACT UBR5 is a nuclear E3 ligase that ubiquitinates vast range of substrates for proteasomal degradation. This HECT has recently been identified as an important regulator oncogenes, e.g., MYC, but little known about its structure or mechanisms substrate engagement and ubiquitination. Here, we present the cryo-EM human UBR5, revealing building block antiparallel dimer which can further assemble into larger oligomers. The large helical scaffold decorated with numerous protein-interacting...
Abstract Nuclear protein homeostasis, including the turnover of transcription factors, critically depends on nuclear proteasomes. After each cell division, proteasomes need to be re-imported into newly formed nucleus in a highly dynamic process that requires largely unstructured AKIRIN2. However, how AKIRIN2 orchestrates this and, more generally, large complexes are translocated remains poorly understood. Here, we have used an integrated approach combining protein-wide saturation mutagenesis...