A5004600651- RNA Research and Splicing
- Peroxisome Proliferator-Activated Receptors
- Fungal and yeast genetics research
- Mitochondrial Function and Pathology
- Nuclear Structure and Function
- RNA modifications and cancer
- Microbial Metabolic Engineering and Bioproduction
- Metabolism and Genetic Disorders
- Biotin and Related Studies
- Cellular transport and secretion
- Genomics and Chromatin Dynamics
- Biofuel production and bioconversion
University of Groningen
2018-2022
University of Exeter
2022
Shanghai Jiao Tong University
2022
Keio University
2022
Estación Experimental del Zaidín
2022
Sanford Burnham Prebys Medical Discovery Institute
2022
Western University
2022
National Centre for Biological Sciences
2022
Heidelberg University
2022
University of California, San Diego
2022
Nuclear transport is facilitated by the Pore Complex (NPC) and essential for life in eukaryotes. The NPC a long-lived exceptionally large structure. We asked whether quality control compromised aging mitotic cells. Our images of single yeast cells during aging, show that abundance several components assembly factors decreases. Additionally, single-cell histories reveal better maintain those are longer lived. presence herniations at nuclear envelope aged suggests misassembled NPCs accumulated...
Using electron and fluorescence microscopy techniques, we identified various physical contacts between peroxisomes other cell organelles in the yeast Hansenula polymorpha. In exponential glucose-grown cells, which typically contain a single small peroxisome, were only observed with endoplasmic reticulum plasma membrane. Here focus on novel peroxisome-vacuole contact site that is formed when cells are shifted to methanol containing media, conditions induce strong peroxisome development. At...
In the yeast Hansenula polymorpha peroxisomal membrane protein Pex11 and three endoplasmic reticulum localized proteins of Pex23 family (Pex23, Pex24 Pex32) are involved in formation peroxisome-ER contact sites. Previous studies suggested that these contacts non-vesicular lipid transfer important for expansion membrane. The absence Pex32 results a severe phenotype, while cells lacking Pex11, or show milder defects still capable to form peroxisomes grow on methanol. We performed transposon...
The yeast Hansenula polymorpha contains four members of the Pex23 family peroxins, which characteristically contain a DysF domain. Here we show that all H. proteins localize to endoplasmic reticulum (ER). Pex24 and Pex32, but not Pex29, predominantly accumulate at peroxisome-ER contacts. Upon deletion PEX24 or PEX32 - much lesser extent, PEX23 PEX29 contacts are lost, concomitant with defects in peroxisomal matrix protein import, membrane growth, organelle proliferation, positioning...
Abstract We analyzed all four Pex23 family proteins of the yeast Hansenula polymorpha , which localize to ER. Of these Pex24 and Pex32, but not Pex29, accumulate at peroxisome-ER contacts, where they are important for normal peroxisome biogenesis proliferation contribute organelle positioning segregation. Upon deletion PEX24 PEX32 - a lesser extent PEX23 PEX29 contacts disrupted, concomitant with peroxisomal defects. These defects suppressed upon introduction an artificial tether....