A5001922195- Ubiquitin and proteasome pathways
- Endoplasmic Reticulum Stress and Disease
- Autophagy in Disease and Therapy
- Cellular transport and secretion
- Glycosylation and Glycoproteins Research
- Protein Degradation and Inhibitors
- Cancer-related Molecular Pathways
- Fungal and yeast genetics research
- Nuclear Structure and Function
- Peptidase Inhibition and Analysis
- Heat shock proteins research
- RNA and protein synthesis mechanisms
- Biochemical Analysis and Sensing Techniques
- Genomics and Chromatin Dynamics
- Genetics, Bioinformatics, and Biomedical Research
- Epigenetics and DNA Methylation
- Microtubule and mitosis dynamics
- RNA Research and Splicing
- Genetics and Neurodevelopmental Disorders
- Photosynthetic Processes and Mechanisms
- Pancreatic function and diabetes
- RNA modifications and cancer
- Histone Deacetylase Inhibitors Research
- Biotechnology and Related Fields
- Scientific Computing and Data Management
Max Delbrück Center
2014-2024
Humboldt-Universität zu Berlin
2010-2024
Friedrich-Alexander-Universität Erlangen-Nürnberg
2001-2020
Technion – Israel Institute of Technology
2013-2020
German Centre for Cardiovascular Research
2019
Justus-Liebig-Universität Gießen
2017-2018
Giessen School of Theology
2018
Quinnipiac University
2013-2014
California State University, San Bernardino
2013
University of Nevada, Las Vegas
2009
Endoplasmic reticulum (ER) degradation of aberrant proteins is mediated by the ubiquitin-proteasome pathway. Here, a membrane-bound component ubiquitin system, Cue1p, was identified. It shown to recruit soluble ubiquitin-conjugating enzyme Ubc7p ER membrane. In absence unassembled and thus cytosolically mislocalized unable participate in or turnover non-ER proteins. Moreover, ubiquitination Cue1p-assembled Ubc6p prerequisite for retrograde transport lumenal substrates out ER, which suggests...
To maintain protein homeostasis in secretory compartments, eukaryotic cells harbor a quality control system that monitors folding and complex assembly the endoplasmic reticulum (ER). Proteins do not fold properly or integrate into cognate complexes are degraded by ER-associated degradation (ERAD) involving retrotranslocation to cytoplasm proteasomal peptide hydrolysis. N-linked glycans essential glycoprotein ERAD; covalent oligosaccharide structure is used as signal display status of host...
Significance A substrate-conjugated polyubiquitin chain is accepted as the “canonical” proteasomal degradation signal. Using a cellular (human and yeast) proteomic screen in exclusive presence of nonpolymerizable ubiquitin, we show that large group proteins degraded by proteasome following monoubiquitination. The also unraveled polyubiquitin-dependent substrates, they are stabilized this ubiquitin mutant. Notably, monoubiquitination- polyubiquitination-dependent substrates display distinct...