Markus Islinger

ORCID: 0000-0001-8881-0902
Publications
Citations
Views
---
Saved
---
About
Contact & Profiles
Research Areas
  • Peroxisome Proliferator-Activated Receptors
  • Adipose Tissue and Metabolism
  • Cancer, Hypoxia, and Metabolism
  • RNA modifications and cancer
  • Metabolism, Diabetes, and Cancer
  • Metabolism and Genetic Disorders
  • Mitochondrial Function and Pathology
  • interferon and immune responses
  • Reproductive biology and impacts on aquatic species
  • Lipid metabolism and biosynthesis
  • Metabolomics and Mass Spectrometry Studies
  • Cellular transport and secretion
  • Ubiquitin and proteasome pathways
  • Genetic and Clinical Aspects of Sex Determination and Chromosomal Abnormalities
  • RNA Research and Splicing
  • Microfluidic and Capillary Electrophoresis Applications
  • Mass Spectrometry Techniques and Applications
  • Aquaculture Nutrition and Growth
  • Sperm and Testicular Function
  • Lipid Membrane Structure and Behavior
  • Fuel Cells and Related Materials
  • Enzyme Catalysis and Immobilization
  • Amino Acid Enzymes and Metabolism
  • Autophagy in Disease and Therapy
  • Neuroscience and Neuropharmacology Research

Heidelberg University
2015-2025

University Hospital Heidelberg
2013-2025

University Medical Centre Mannheim
2014-2025

Bernstein Center for Computational Neuroscience Heidelberg-Mannheim
2022

Assiut University
2022

University of Mannheim
2020

University of Aveiro
2011-2014

Heidelberg University
2008-2012

Zero to Three
2009

Vrije Universiteit Amsterdam
2009

Peroxisomes (POs) and the endoplasmic reticulum (ER) cooperate in cellular lipid metabolism form tight structural associations, which were first observed ultrastructural studies decades ago. PO-ER associations have been suggested to impact on a diverse number of physiological processes, including metabolism, phospholipid exchange, metabolite transport, signaling, PO biogenesis. Despite their fundamental importance cell mechanisms by regions ER become tethered POs are unknown, particular...

10.1083/jcb.201607055 article EN cc-by The Journal of Cell Biology 2017-01-20

Scientific Report12 June 2018Open Access Source DataTransparent process Dual role of USP30 in controlling basal pexophagy and mitophagy Elena Marcassa Cellular Molecular Physiology, Institute Translational Medicine, University Liverpool, UK Search for more papers by this author Andreas Kallinos Jane Jardine Emma V Rusilowicz-Jones Aitor Martinez Sandra Kuehl Neuroanatomy, Centre Biomedicine Medical Technology Mannheim, Faculty Heidelberg, Germany Markus Islinger Michael J Clague...

10.15252/embr.201745595 article EN cc-by EMBO Reports 2018-06-12

Tail-anchored (TA) proteins contain a single transmembrane domain (TMD) at the C-terminus that anchors them to membranes of organelles where they mediate critical cellular processes. Accordingly, mutations in genes encoding TA have been identified number severe inherited disorders. Despite importance correctly targeting protein its appropriate membrane, mechanisms and signals involved are not fully understood. In this study, we identify additional peroxisomal proteins, discover more present...

10.1242/jcs.200204 article EN cc-by Journal of Cell Science 2017-03-22

Most newly synthesized peroxisomal proteins are imported in a receptor-mediated fashion, depending on the interaction of targeting signal (PTS) with its cognate receptor Pex5 or Pex7 located cytoplasm. Apart from this classic mechanism, heterologous protein complexes that have been proposed more than decade ago also to be into peroxisomes. However, it remains still unclear if so-called piggyback import is physiological relevance mammals. Here, we show Cu/Zn superoxide dismutase 1 (SOD1), an...

10.1111/j.1600-0854.2009.00966.x article EN Traffic 2009-07-21

Fibrates are known to induce peroxisome proliferation and the expression of peroxisomal β-oxidation enzymes. To analyze fibrate-induced changes complex metabolic networks, we have compared proteome rat liver peroxisomes from control bezafibrate-treated rats. Highly purified were subfractionated, proteins matrix, peripheral, integral membrane subfractions thus obtained analyzed by matrix-assisted laser desorption ionization time-of-flight/time-of-flight mass spectrometry after labeling...

10.1074/jbc.m610910200 article EN cc-by Journal of Biological Chemistry 2007-05-24

Cooperation between cellular organelles such as mitochondria, peroxisomes and the ER is essential for a variety of important diverse metabolic processes. Effective communication metabolite exchange requires physical linkages organelles, predominantly in form organelle contact sites. At sites membranes are brought into close proximity by action molecular tethers, which often consist specific protein pairs anchored membrane opposing organelles. Currently numerous tethering components have been...

10.1080/15384101.2017.1314422 article EN cc-by Cell Cycle 2017-05-02

Ongoing technical and bioinformatics improvements in mass spectrometry (MS) allow for the identifying quantifying of enrichment increasingly less-abundant proteins individual fractions. Accordingly, this study reassessed proteome mouse liver peroxisomes by parallel isolation from a mitochondria- microsome-enriched prefraction, combining density-gradient centrifugation with semi-quantitative SWATH-MS proteomics approach to unveil novel peroxisomal or peroxisome-associated proteins. In total,...

10.3390/cells13020176 article EN cc-by Cells 2024-01-17

Abstract The human cytomegalovirus developed distinct evasion mechanisms from the cellular antiviral response involving vMIA, a virally-encoded protein that is not only able to prevent apoptosis but also inhibit signalling downstream mitochondrial MAVS. vMIA has been shown localize at mitochondria and trigger their fragmentation, phenomenon proven be essential for inhibition. Here, we demonstrate localized peroxisomes, induces fragmentation inhibits peroxisomal-dependent pathway....

10.1038/srep26028 article EN cc-by Scientific Reports 2016-05-16

Peroxisome membrane dynamics and division are essential to adapt the peroxisomal compartment cellular needs. The protein PEX11β (also known as PEX11B) tail-anchored adaptor proteins FIS1 (mitochondrial fission 1) MFF factor), which recruit GTPase DRP1 (dynamin-related 1, also DNML1) both peroxisomes mitochondria, key factors of division. current model suggests that is for peroxisome division, whereas role unclear. Here, we reveal can promote in absence a DRP1- FIS1-dependent manner. We...

10.1242/jcs.259924 article EN cc-by Journal of Cell Science 2022-06-09
Coming Soon ...