Natalia H. Revelo

Radboud Institute for Molecular Life Sciences

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Geert van den Bogaart

University of Groningen

Martin ter Beest

Radboud University Nijmegen

Silvio O. Rizzoli

Universitätsmedizin Göttingen

Daniëlle R. J. Verboogen

Elisabeth-TweeSteden Ziekenhuis

Peter Linders

Radboud University Nijmegen

Dirk J. Lefeber

Radboud University Nijmegen

Melissa Baerenfaenger

Radboud University Nijmegen

Richard Arts

Radboud University Medical Center

KÕ

Katrin Õunap

University of Tartu

Karin Huijben

Radboud University Nijmegen

Cooperative Institutions

University of Göttingen

Universitätsmedizin Göttingen

University Medical Center

Radboud University Nijmegen

Radboud University Medical Center

Radboud Institute for Molecular Life Sciences

Nanoscale Microscopy and Molecular Physiology of the Brain Cluster of Excellence 171 — DFG Research Center 103

Max Planck Institute for Biophysical Chemistry

University of Groningen

Max Planck Institute for Multidisciplinary Sciences

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SWAP70 Organizes the Actin Cytoskeleton and Is Essential for Phagocytosis

Cell Reports (2016)

Maksim V. Baranov Natalia H. Revelo Ilse Dingjan Riccardo Maraspini Martin ter Beest

Actin plays a critical role during the early stages of pathogenic microbe internalization by immune cells. In this study, we identified a key mechanism of actin filament tethering and stabilization to the surface of phagosomes in human dendritic cells. We found that the actin-binding protein SWAP70 is specifically recruited to nascent phagosomes by binding to the lipid phosphatidylinositol (3,4)-bisphosphate. Multi-color super-resolution stimulated emission depletion (STED) microscopy revealed that the actin cage surrounding early phagosomes is formed by multiple concentric rings containing SWAP70. SWAP70 colocalized with and stimulated activation of RAC1, a known activator of actin polymerization, on phagosomes. Genetic ablation of SWAP70 impaired actin polymerization around phagosomes and resulted in a phagocytic defect. These data show a key role for SWAP70 as a scaffold for tethering the peripheral actin cage to phagosomes.

Internalization

Actin remodeling

Lamellipodium

10.1016/j.celrep.2016.10.021

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Citations (56)

Optical Dissection of Experience-Dependent Pre- and Postsynaptic Plasticity in the Drosophila Brain

Cell Reports (2015)

Ulrike Pech Natalia H. Revelo Katharina J. Seitz Silvio O. Rizzoli André Fiala

Drosophila represents a key model organism for dissecting neuronal circuits that underlie innate and adaptive behavior. However, this task is limited by a lack of tools to monitor physiological parameters of spatially distributed, central synapses in identified neurons. We generated transgenic fly strains that express functional fluorescent reporters targeted to either pre- or postsynaptic compartments. Presynaptic Ca2+ dynamics are monitored using synaptophysin-coupled GCaMP3, synaptic transmission is monitored using red fluorescent synaptophysin-pHTomato, and postsynaptic Ca2+ dynamics are visualized using GCaMP3 fused with the postsynaptic matrix protein, dHomer. Using two-photon in vivo imaging of olfactory projection neurons, odor-evoked activity across populations of synapses is visualized in the antennal lobe and the mushroom body calyx. Prolonged odor exposure causes odor-specific and differential experience-dependent changes in pre- and postsynaptic activity at both levels of olfactory processing. The approach advances the physiological analysis of synaptic connections across defined groups of neurons in intact Drosophila.

Mushroom bodies

Antennal lobe

Postsynaptic density

Synaptophysin

Biological neural network

10.1016/j.celrep.2015.02.065

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Citations (73)

CD14 and TRIF govern distinct responsiveness and responses in mouse microglial TLR4 challenges by structural variants of LPS

Brain Behavior and Immunity (2010)

Tommy Regen Denise van Rossum Jörg Scheffel Maria Eleni Kastriti Natalia H. Revelo

TRIF

10.1016/j.bbi.2010.10.009

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Citations (67)

Congenital disorder of glycosylation caused by starting site-specific variant in syntaxin-5

Zenodo (CERN European Organization for Nuclear Research) (2021)

Peter Linders Eveline Gerretsen Angel Ashikov Mari‐Anne Vals Rinse de Boer

The SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) protein syntaxin-5 (Stx5) is essential for Golgi transport. In humans, the STX5 mRNA encodes two protein isoforms, Stx5 Long (Stx5L) from the first starting methionine and Stx5 Short (Stx5S) from an alternative starting methionine at position 55. In this study, we identified a novel human disorder caused by a single missense substitution in the second starting methionine (p.M55V), resulting in complete loss of the short isoform. Patients suffer from an early fatal multisystem disease, including severe liver disease, skeletal abnormalities and abnormal glycosylation. Primary human dermal fibroblasts isolated from these patients showed defective glycosylation, altered Golgi morphology as measured by electron microscopy and mislocalization of glycosyltransferases. Measurements of anterograde trafficking, based on biotin-synchronizable forms of Stx5 (the RUSH system), and of cognate binding SNAREs, based on Förster resonance energy transfer (FRET), revealed that the short isoform of Stx5 is essential for intra-Golgi transport. This is the first time a mutation in an alternative starting codon is linked to human disease, demonstrating that the site of translation initiation is an important new layer of regulating protein trafficking.

10.5281/zenodo.4638787

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A positive feedback loop of IL-12 and IFN-gamma signaling potentiates both CD8+T cell and DC activation

Elke Muntjewerff Natalia H. Revelo Geert van den Bogaart

Positive feedback

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Endosomal and Phagosomal SNAREs

Physiological Reviews (2018)

Ilse Dingjan Peter Linders Daniëlle R. J. Verboogen Natalia H. Revelo Martin ter Beest

The soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) protein family is of vital importance for organelle communication. The complexing of cognate SNARE members present in both the donor and target organellar membranes drives the membrane fusion required for intracellular transport. In the endocytic route, SNARE proteins mediate trafficking between endosomes and phagosomes with other endosomes, lysosomes, the Golgi apparatus, the plasma membrane, and the endoplasmic reticulum. The goal of this review is to provide an overview of the SNAREs involved in endosomal and phagosomal trafficking. Of the 38 SNAREs present in humans, 30 have been identified at endosomes and/or phagosomes. Many of these SNAREs are targeted by viruses and intracellular pathogens, which thereby reroute intracellular transport for gaining access to nutrients, preventing their degradation, and avoiding their detection by the immune system. A fascinating picture is emerging of a complex transport network with multiple SNAREs being involved in consecutive trafficking routes.

Transport protein

Retromer

Rab

Vesicular Transport Proteins

SNARE complex

Endomembrane system

10.1152/physrev.00037.2017

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Citations (96)

SWAP70 is a universal GEF-like adaptor for tethering actin to phagosomes

Small GTPases (2017)

Maksim V. Baranov Natalia H. Revelo Daniëlle R. J. Verboogen Martin ter Beest Geert van den Bogaart

We recently identified a key role for SWAP70 as the tethering factor stabilizing F-actin filaments on the surface of phagosomes in human dendritic cells by interacting both with Rho-family GTPases and the lipid phosphatidylinositol (3,4)-bisphosphate. In this study, we aimed to investigate whether this role of SWAP70 was general among immune phagocytes. Our data reveal that SWAP70 is recruited to early phagosomes of macrophages and dendritic cells from both human and mouse. The putative inhibitor of SWAP70 sanguinarine blocked phagocytosis and F-actin polymerization, supporting a key role for SWAP70 in phagocytosis as demonstrated previously with knock-down. Moreover, SWAP70 was recently shown to sequester the F-actin severing protein cofilin and we investigated this relationship in phagocytosis. Our data show an increased activation of cellular cofilin upon siRNA knockdown of SWAP70. Finally, we explored whether SWAP70 would be recruited to the immune synapse between dendritic cells and T cells required for antigen presentation, as the formation of such synapses depends on F-actin. However, we observed that SWAP70 was depleted at immune synapses and specifically was recruited to phagosomes. Our data support an essential and specific role for SWAP70 in tethering and stabilizing F-actin to the phagosomal surface in a wide range of phagocytes.

Cofilin

Immunological synapse

Pseudopodia

Rac GTP-Binding Proteins

10.1080/21541248.2017.1328302

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Citations (8)

Application of STED Microscopy to Cell Biology Questions

Methods in molecular biology (2014)

Natalia H. Revelo Silvio O. Rizzoli

STED microscopy

10.1007/978-1-4939-2080-8_12

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Citations (11)

Novel and conventional inhibitors of canonical autophagy differently affect LC3-associated phagocytosis

Zenodo (CERN European Organization for Nuclear Research) (2021)

Femmy C. Stempels M.H. Janssens Martin ter Beest Rob Mesman Natalia H. Revelo

Affect

Non canonical

10.5281/zenodo.5714530

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The Membrane Marker mCLING Reveals the Molecular Composition of Trafficking Organelles

Current Protocols in Neuroscience (2016)

Natalia H. Revelo Silvio O. Rizzoli

Abstract mCLING is a fixable endocytosis marker that can be combined with immunolabeling techniques to study the molecular composition of trafficking organelles. mCLING can be used both in cultured cells and in tissue if critical sample preparation steps, such as fixation, are correctly performed. This unit describes protocols for the application of mCLING and for the subsequent sample processing. We include immunostaining protocols and embedding procedures for confocal and high‐resolution microscopy. © 2016 by John Wiley & Sons, Inc.

Immunolabeling

Organelle

Immunostaining

10.1002/0471142301.ns0225s74

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Citations (21)