Walter Neupert

ORCID: 0000-0003-0571-4419
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About
Contact & Profiles
Research Areas
  • Mitochondrial Function and Pathology
  • ATP Synthase and ATPases Research
  • RNA and protein synthesis mechanisms
  • Photosynthetic Processes and Mechanisms
  • Metabolism and Genetic Disorders
  • Heat shock proteins research
  • Protein Structure and Dynamics
  • RNA modifications and cancer
  • Endoplasmic Reticulum Stress and Disease
  • Lipid Membrane Structure and Behavior
  • Fungal and yeast genetics research
  • Enzyme Structure and Function
  • Microbial Metabolic Engineering and Bioproduction
  • Genomics and Phylogenetic Studies
  • Metabolomics and Mass Spectrometry Studies
  • Trace Elements in Health
  • RNA Research and Splicing
  • Bacterial Genetics and Biotechnology
  • Hemoglobin structure and function
  • Peptidase Inhibition and Analysis
  • Ubiquitin and proteasome pathways
  • Metalloenzymes and iron-sulfur proteins
  • Biotin and Related Studies
  • Signaling Pathways in Disease
  • Genetic Neurodegenerative Diseases

Ludwig-Maximilians-Universität München
2008-2024

LMU Klinikum
2009-2024

Max Planck Institute of Biochemistry
2009-2019

Max Planck Institute of Psychiatry
2015

Max Planck Society
2010-2015

Center for Integrated Protein Science Munich
2008-2012

Institut für Urheber- und Medienrecht
2002

Columbia University
2000

Marquette University
2000

University of Alberta
1995-1998

The understanding of the processes underlying organellar function and inheritance requires identification characterization molecular components involved. We pursued a genomic approach to define complements genes required for respiratory growth mitochondria with normal morphology in yeast. With systematic screening deletion mutant library covering nonessential Saccharomyces cerevisiae numbers known be establishment wild-type-like mitochondrial structure have been more than doubled. In...

10.1091/mbc.01-12-0588 article EN Molecular Biology of the Cell 2002-03-01

Many muscular and neurological disorders are associated with mitochondrial dysfunction often accompanied by changes in morphology. Mutations the gene encoding OPA1, a protein required for fusion of mitochondria, hereditary autosomal dominant optic atrophy type I. Here we show that fragmentation correlates processing large isoforms OPA1 cybrid cells from patient myoclonus epilepsy ragged-red fibers syndrome mouse embryonic fibroblasts harboring an error-prone mtDNA polymerase gamma....

10.1074/jbc.m606059200 article EN cc-by Journal of Biological Chemistry 2006-09-27

The inner membrane of mitochondria is organized in two morphologically distinct domains, the boundary (IBM) and cristae (CM), which are connected by narrow, tubular junctions. protein composition these their dynamics, biogenesis maintenance poorly understood at molecular level. We have used quantitative immunoelectron microscopy to determine distribution a collection representative proteins yeast belonging seven major processes: oxidative phosphorylation, translocation, metabolite exchange,...

10.1083/jcb.200605138 article EN The Journal of Cell Biology 2006-10-16

The structure of mitochondria is highly dynamic and depends on the balance fusion fission processes. Deletion mitochondrial dynamin-like protein Mgm1 in yeast leads to extensive fragmentation loss DNA. its human ortholog OPA1, associated with optic atrophy type I humans, were proposed be involved or or, alternatively, remodeling inner membrane cristae formation (Wong, E. D., Wagner, J. A., Gorsich, S. W., McCaffery, M., Shaw, Nunnari, (2000) Cell Biol. 151, 341-352; Wong, Scott, V.,...

10.1074/jbc.m211311200 article EN cc-by Journal of Biological Chemistry 2003-07-01

Crista junctions (CJs) are important for mitochondrial organization and function, but the molecular basis of their formation architecture is obscure. We have identified characterized a membrane protein in yeast, Fcj1 (formation CJ 1), which specifically enriched CJs. Cells lacking lack CJs, exhibit concentric stacks inner matrix, show increased levels F1FO–ATP synthase (F1FO) supercomplexes. Overexpression leads to formation, branching cristae, enlargement diameter, reduced F1FO Impairment...

10.1083/jcb.200811099 article EN cc-by-nc-sa The Journal of Cell Biology 2009-06-15

The mitochondrial inner membrane contains a large protein complex that functions in organization and formation of contact sites. was variably named the site complex, organizing system, structure, or Mitofilin/Fcj1 complex. To facilitate future studies, we propose to unify nomenclature term "mitochondrial cristae system" its subunits Mic10 Mic60.

10.1083/jcb.201401006 article EN cc-by-nc-sa The Journal of Cell Biology 2014-03-31

We describe the construction and characterization of a novel set plasmids for expression mitochondria-targeted green fluorescent protein (GFP) in Saccharomyces cerevisiae. The vectors include constructs with strong regulatable constitutive promoters, four different auxotrophic markers yeast transformation, (S65T) blue-shifted (P4-3) variant GFP. Mitochondria are brightly living cells grown on carbon sources at temperatures, virtually no background staining. Specific staining mitochondria is...

10.1002/1097-0061(200011)16:15<1421::aid-yea624>3.0.co;2-u article EN Yeast 2000-01-01

Fzo1p is a novel component required for the biogenesis of functional mitochondria in yeast Saccharomyces cerevisiae. The protein homologous to DrosophilaFzo, first known mediator mitochondrial fusion. Deletion FZO1 gene results petite phenotype, loss DNA, and fragmented morphology. an integral outer membrane exposing its major part cytosol. It imported into receptor-dependent manner. larger complex 800 kDa, presumably identified fusion machinery. Mitochondria exist particular cell type...

10.1074/jbc.273.32.20150 article EN cc-by Journal of Biological Chemistry 1998-08-01

Prohibitins comprise a protein family in eukaryotic cells with potential roles senescence and tumor suppression. Phb1p Phb2p, members of the prohibitin Saccharomyces cerevisiae, have been implicated regulation replicative life span maintenance mitochondrial morphology. The functional activities these proteins, however, not elucidated. We demonstrate here that prohibitins regulate turnover membrane proteins by m-AAA protease, conserved ATP-dependent protease inner mitochondria. is composed...

10.1128/mcb.19.5.3435 article EN Molecular and Cellular Biology 1999-05-01
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