Wolfgang Staroske

TU Dresden

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Petra Schwille

Max Planck Institute of Biochemistry

Thomas Ohrt

Max Planck Institute for Biophysical Chemistry

Stefanie Kretschmer

TU Dresden

Franz Kapplusch

University Hospital Carl Gustav Carus

Alexander Rapp

Technical University of Darmstadt

M. Cristina Cardoso

Technical University of Darmstadt

Angela Rösen‐Wolff

University Hospital Carl Gustav Carus

Robert Stein

University Hospital Leipzig

Jörg Mütze

Siemens (Germany)

Karin Crell

TU Dresden

Cooperative Institutions

TU Dresden

University Hospital Carl Gustav Carus

Klinik und Poliklinik für Kinder- und Jugendmedizin

Max Planck Society

Max Planck Institute of Biochemistry

Technical University of Darmstadt

Ludwig-Maximilians-Universität München

Center for Systems Biology Dresden

Heinrich Heine University Düsseldorf

Klinik und Poliklinik für Psychotherapie und Psychosomatik

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Phospho-NHE3 forms membrane patches and interacts with beta-actin to sense and maintain constant direction during cell migration

Experimental Cell Research (2014)

Srikanth Perike Nurdan Özkucur Priyanka Sharma Wolfgang Staroske Robert Bläsche

Cytochalasin D

10.1016/j.yexcr.2014.03.005

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Citations (15)

Enzymatically Inactive Procaspase 1 stabilizes the ASC Pyroptosome and Supports Pyroptosome Spreading during Cell Division

Journal of Biological Chemistry (2016)

Robert Stein Franz Kapplusch Michael C. Heymann Susanne Ruß Wolfgang Staroske

Pyroptosis

AIM2

Caspase 8

10.1074/jbc.m116.718668

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Citations (14)

Influence of the naturally occurring human CASP1 variant L265S on subcellular distribution and pyroptosis

Pediatric Rheumatology (2015)

S Rabe MC Heymann Robert Stein Franz Kapplusch S. Russ

Patients with unexplained recurrent febrile episodes and CASP1 variants suffer from systemic sterile inflammation despite altered enzymatic activity of procaspase-1 and reduced IL-1β release. Most recent findings from our group indicate that the proinflammatory effects of CASP1 variants with reduced or abrogated enzymatic activity could be due to receptor interacting protein kinase 2 (RIP2) mediated increase of NF-kB activation. These findings are additionally supported by a trend to elevated IL-6 and TNF-α expression in patients with CASP1 variants.

Pyroptosis

10.1186/1546-0096-13-s1-o61

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Nuclear RISC Originates from Cytoplasmic Loaded RISC in Human Cells

Biophysical Journal (2009)

Joerg Muetze Thomas Ohrt Wolfgang Staroske Karin Crell Petra Schwille

RNA-induced silencing complex

Argonaute

10.1016/j.bpj.2008.12.223

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Enzymatically inactive procaspase-1 stabilizes the ASC-pyroptosome

Pediatric Rheumatology (2015)

Robert Stein MC Heymann Franz Kapplusch S. Russ Wolfgang Staroske

Caspase-1 (or interleukin-1 converting enzyme, ICE) plays an important role in mediating proinflammatory innate immune responses, especially by activation of pro-IL-1s within inflammasomes. Some patients with recurrent febrile episodes and systemic inflammation of yet unknown origin harbor CASP1-mutations with incomplete penetrance. These CASP1-variants cause reduced enzymatic activity of procaspase-1 and less IL-1s secretion.

Proinflammatory cytokine

10.1186/1546-0096-13-s1-o79

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Citations (1)

RPA and Rad51 constitute a cell intrinsic mechanism to protect the cytosol from self DNA

Nature Communications (2016)

Christine Wolf Alexander Rapp Nicole Berndt Wolfgang Staroske Max Schuster

Abstract Immune recognition of cytosolic DNA represents a central antiviral defence mechanism. Within the host, short single-stranded DNA (ssDNA) continuously arises during the repair of DNA damage induced by endogenous and environmental genotoxic stress. Here we show that short ssDNA traverses the nuclear membrane, but is drawn into the nucleus by binding to the DNA replication and repair factors RPA and Rad51. Knockdown of RPA and Rad51 enhances cytosolic leakage of ssDNA resulting in cGAS-dependent type I IFN activation. Mutations in the exonuclease TREX1 cause type I IFN-dependent autoinflammation and autoimmunity. We demonstrate that TREX1 is anchored within the outer nuclear membrane to ensure immediate degradation of ssDNA leaking into the cytosol. In TREX1-deficient fibroblasts, accumulating ssDNA causes exhaustion of RPA and Rad51 resulting in replication stress and activation of p53 and type I IFN. Thus, the ssDNA-binding capacity of RPA and Rad51 constitutes a cell intrinsic mechanism to protect the cytosol from self DNA.

Replication protein A

10.1038/ncomms11752

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Citations (144)

Fluorescence Cross-Correlation Spectroscopy Reveals Mechanistic Insights into the Effect of 2′-O-Methyl Modified siRNAs in Living Cells

Biophysical Journal (2011)

Thomas Ohrt Wolfgang Staroske Jörg Mütze Karin Crell Markus Landthaler

Fluorescence Correlation Spectroscopy

10.1016/j.bpj.2011.05.005

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Citations (15)

Fluorescence Correlation Spectroscopy Elucidates the Pathway of RNA Interference

Biophysical Journal (2010)

Jörg Mütze Thomas Ohrt Wolfgang Staroske Lasse Weinmann Julia Höck

Argonaute

RNA-induced silencing complex

RNA Silencing

Trans-acting siRNA

RNA-induced transcriptional silencing

10.1016/j.bpj.2009.12.2232

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Single-stranded nucleic acids promote SAMHD1 complex formation

Journal of Molecular Medicine (2013)

Victoria Tüngler Wolfgang Staroske Barbara Kind Manuela Dobrick Stefanie Kretschmer

SAMHD1

Nucleic acid structure

10.1007/s00109-013-0995-3

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Citations (73)

Fluorescence correlation spectroscopy and fluorescence cross-correlation spectroscopy reveal the cytoplasmic origination of loaded nuclear RISC in vivo in human cells

Nucleic Acids Research (2008)

Thomas Ohrt Jörg Mütze Wolfgang Staroske Lasse Weinmann Julia Höck

Studies of RNA interference (RNAi) provide evidence that in addition to the well-characterized cytoplasmic mechanisms, nuclear mechanisms also exist. The mechanism by which the nuclear RNA-induced silencing complex (RISC) is formed in mammalian cells, as well as the relationship between the RNA silencing pathways in nuclear and cytoplasmic compartments is still unknown. Here we show by applying fluorescence correlation and cross-correlation spectroscopy (FCS/FCCS) in vivo that two distinct RISC exist: a large approximately 3 MDa complex in the cytoplasm and a 20-fold smaller complex of approximately 158 kDa in the nucleus. We further show that nuclear RISC, consisting only of Ago2 and a short RNA, is loaded in the cytoplasm and imported into the nucleus. The loaded RISC accumulates in the nucleus depending on the presence of a target, based on an miRNA-like interaction with impaired cleavage of the cognate RNA. Together, these results suggest a new RISC shuttling mechanism between nucleus and cytoplasm ensuring concomitant gene regulation by small RNAs in both compartments.

RNA-induced silencing complex

Argonaute

10.1093/nar/gkn693

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Citations (183)