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5. IntAct: A nondisruptive internal tagging strategy to study the organization and function of actin isoforms.

Author

van Zwam, Maxime C., Dhar, Anubhav, Bosman, Willem, van Straaten, Wendy, Weijers, Suzanne, Seta, Emiel, Joosten, Ben, van Haren, Jeffrey, Palani, Saravanan, and van den Dries, Koen

Subjects
ACTIN, MICROFILAMENT proteins, MOLECULAR interactions, MOLECULAR dynamics, CELL lines, CO-cultures, ANIMAL species
Abstract

Mammals have 6 highly conserved actin isoforms with nonredundant biological functions. The molecular basis of isoform specificity, however, remains elusive due to a lack of tools. Here, we describe the development of IntAct, an internal tagging strategy to study actin isoforms in fixed and living cells. We identified a residue pair in β-actin that permits tag integration and used knock-in cell lines to demonstrate that IntAct β-actin expression and filament incorporation is indistinguishable from wild type. Furthermore, IntAct β-actin remains associated with common actin-binding proteins (ABPs) and can be targeted in living cells. We demonstrate the usability of IntAct for actin isoform investigations by showing that actin isoform-specific distribution is maintained in human cells. Lastly, we observed a variant-dependent incorporation of tagged actin variants into yeast actin patches, cables, and cytokinetic rings demonstrating cross species applicability. Together, our data indicate that IntAct is a versatile tool to study actin isoform localization, dynamics, and molecular interactions. Mammals have six highly-conserved actin isoforms with nonredundant functions, but their molecular properties remain unknown. These authors develop IntAct, a versatile tool to study actin isoform localization, dynamics and molecular interactions across species in both fixed an living cells. [ABSTRACT FROM AUTHOR]

Published
2024
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10. Cellular Uptake of Modified Mesoporous Bioactive Glass Nanoparticles for Effective Intracellular Delivery of Therapeutic Agents

Author

Hassani Besheli,Negar, Verbakel,Juul, Hosseini,Maryam, Andrée,Lea, Joosten,Ben, Walboomers,X Frank, Cambi,Alessandra, Yang,Fang, Leeuwenburgh,Sander CG, Hassani Besheli,Negar, Verbakel,Juul, Hosseini,Maryam, Andrée,Lea, Joosten,Ben, Walboomers,X Frank, Cambi,Alessandra, Yang,Fang, and Leeuwenburgh,Sander CG

Abstract

Negar Hassani Besheli,1 Juul Verbakel,1 Maryam Hosseini,1 Lea Andrée,1 Ben Joosten,2 X Frank Walboomers,1 Alessandra Cambi,2 Fang Yang,1 Sander CG Leeuwenburgh1 1Department of Dentistry – Regenerative Biomaterials, Radboud Institute for Molecular Life Sciences, Radboudumc, Nijmegen, The Netherlands; 2Department of Cell Biology, Radboud Institute for Molecular Life Sciences, Radboudumc, Nijmegen, The NetherlandsCorrespondence: Sander CG Leeuwenburgh, Tel +31 6 15 40 9006, Fax +31 2 43 61 4657, Email sander.leeuwenburgh@radboudumc.nlIntroduction: There has recently been a surge of interest in mesoporous bioactive glass nanoparticles (MBGNs) as multi-functional nanocarriers for application in bone-reconstructive and -regenerative surgery. Their excellent control over their structural and physicochemical properties renders these nanoparticles suitable for the intracellular delivery of therapeutic agents to combat degenerative bone diseases, such as bone infection, or bone cancer. Generally, the therapeutic efficacy of nanocarriers strongly depends on the efficacy of their cellular uptake, which is determined by numerous factors including cellular features and the physicochemical characteristics of nanocarriers, particularly surface charge. In this study, we have systematically investigated the effect of the surface charge of MBGNs doped with copper as a model therapeutic agent on cellular uptake by both macrophages and pre-osteoblast cells involved in bone healing and bone infections to guide the future design of MBGN-based nanocarriers.Methods: Cu-MBGNs with negative, neutral, and positive surface charges were synthesized and their cellular uptake efficiency was assessed. Additionally, the intracellular fate of internalized nanoparticles along with their ability to deliver therapeutic cargo was studied in detail.Results: The results showed that both cell types internalized Cu-MBGNs regardless of their surface charge, indicating that cellular uptake of nanoparticles

Published
2023

17. Microdomains of the C-type lectin DC-SIGN are portals for virus entry into dendritic cells

Author

Cambi, Alessandra, de Lange, Frank, van Maarseveen, Noortje M., Nijhuis, Monique, Joosten, Ben, van Dijk, Erik M.H.P., de Bakker, Barbel I., Fransen, Jack A.M., Bovee-Geurts, Petra H.M., Van Leeuwen, Frank N., van Hulst, Niek F., and Figdor, Carl G.

Subjects
Dendritic cells -- Research, Biological sciences
Abstract

The C-type lectin dendritic cell (DC)-specific inter-cellular adhesion molecule grabbing non-integrin (DC-SIGN; CD209) facilitates binding and internalization of several viruses, including HIV-1, on DCs, but the underlying mechanism for being such an efficient phagocytic pathogen-recognition receptor is poorly understood. By high resolution electron microscopy, we demonstrate a direct relation between DC-SIGN function as viral receptor and its microlocalization on the plasma membrane. During development of human monocyte-derived DCs, DC-SIGN becomes organized in well-defined microdomains, with an average diameter of 200 nm. Biochemical experiments and confocal microscopy indicate that DC-SIGN microdomains reside within lipid rafts. Finally, we show that the organization of DC-SIGN in microdomains on the plasma membrane is important for binding and internalization of virus particles, suggesting that these multimolecular assemblies of DC-SIGN act as a docking site for pathogens like HIV-1 to invade the host.

Published
2004

21. Modular actin nano-architecture enables podosome protrusion and mechanosensing

Author

Dries, K. van den, Nahidiazar, Leila, Slotman, Johan A., Meddens, Marjolein B. M., Pandzic, Elvis, Joosten, Ben, Ansems, M., Fransen, J.A., Jalink, Kees, Cambi, A., Dries, K. van den, Nahidiazar, Leila, Slotman, Johan A., Meddens, Marjolein B. M., Pandzic, Elvis, Joosten, Ben, Ansems, M., Fransen, J.A., Jalink, Kees, and Cambi, A.

Abstract

Contains fulltext : 212261.pdf (publisher's version ) (Open Access)

Published
2019

22. Intracellular Galectin-9 controls dendritic cell function by maintaining plasma membrane rigidity

Author

Cano, Laia Querol, primary, Tagit, Oya, additional, van Duffelen, Anne, additional, Dieltjes, Shannon, additional, Buschow, Sonja I., additional, Niki, Toshiro, additional, Hirashima, Mitsuomi, additional, Joosten, Ben, additional, van den Dries, Koen, additional, Cambi, Alessandra, additional, Figdor, Carl G., additional, and van Spriel, Annemiek B., additional

Published
2019
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23. Synthetic Semiflexible and Bioactive Brushes

Author

Voerman, Dion, primary, Schluck, Marjolein, additional, Weiden, Jorieke, additional, Joosten, Ben, additional, Eggermont, Loek J., additional, van den Eijnde, Tuur, additional, Ignacio, Bob, additional, Cambi, Alessandra, additional, Figdor, Carl G., additional, Kouwer, Paul H. J., additional, Verdoes, Martijn, additional, Hammink, Roel, additional, and Rowan, Alan E., additional

Published
2019
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24. Modular actin nano-architecture enables podosome protrusion and mechanosensing

Author

van den Dries, Koen, primary, Nahidiazar, Leila, additional, Slotman, Johan A., additional, Meddens, Marjolein B.M., additional, Pandzic, Elvis, additional, Joosten, Ben, additional, Ansems, Marleen, additional, Schouwstra, Joost, additional, Meijer, Anke, additional, Steen, Raymond, additional, Wijers, Mietske, additional, Fransen, Jack, additional, Houtsmuller, Adriaan B., additional, Wiseman, Paul W., additional, Jalink, Kees, additional, and cambi, Alessandra, additional

Published
2019
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25. Biophysical Characterization of CD6—TCR/CD3 Interplay in T Cells

Author

Meddens, Marjolein B. M., primary, Mennens, Svenja F. B., additional, Celikkol, F. Burcu, additional, te Riet, Joost, additional, Kanger, Johannes S., additional, Joosten, Ben, additional, Witsenburg, J. Joris, additional, Brock, Roland, additional, Figdor, Carl G., additional, and Cambi, Alessandra, additional

Published
2018
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29. Actomyosin-dependent dynamic spatial patterns of cytoskeletal components drive mesoscale podosome organization

Author

Meddens, Marjolein B. M., primary, Pandzic, Elvis, additional, Slotman, Johan A., additional, Guillet, Dominique, additional, Joosten, Ben, additional, Mennens, Svenja, additional, Paardekooper, Laurent M., additional, Houtsmuller, Adriaan B., additional, van den Dries, Koen, additional, Wiseman, Paul W., additional, and Cambi, Alessandra, additional

Published
2016
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30. CLEC12A-Mediated Antigen Uptake and Cross-Presentation by Human Dendritic Cell Subsets Efficiently Boost Tumor-Reactive T Cell Responses

Author

Hutten, Tim J. A., primary, Thordardottir, Soley, additional, Fredrix, Hanny, additional, Janssen, Lisanne, additional, Woestenenk, Rob, additional, Tel, Jurjen, additional, Joosten, Ben, additional, Cambi, Alessandra, additional, Heemskerk, Mirjam H. M., additional, Franssen, Gerben M., additional, Boerman, Otto C., additional, Bakker, Lex B. H., additional, Jansen, Joop H., additional, Schaap, Nicolaas, additional, Dolstra, Harry, additional, and Hobo, Willemijn, additional

Published
2016
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31. From Nanoscale to Mesoscale: Integrating Advanced Microscopy Techniques to Reveal the Ultrastructure and Coordinated Dynamics of Mechanosensory Podosomes

Author

van den Dries, Koen, primary, Meddens, Marjolein B.M., additional, Pandzic, Elvis, additional, Joosten, Ben, additional, Slotman, Johan A., additional, Nahidiazar, Leila, additional, Jalink, Kees, additional, Houtsmuller, Adriaan B., additional, Wisemann, Paul W., additional, and Cambi, Alessandra, additional

Published
2016
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32. Vivace: .

Author

Woude, Hanne van der, Joosten, Egbert, Eerdmans, Emmy, 1931, Joosten, Ben, Woude, Hanne van der, Joosten, Egbert, Eerdmans, Emmy, 1931, and Joosten, Ben

Abstract

Joan Flasch Artists' Book Collection

Published
2015

35. Dendritic cell Migration on Suspended Non-electrospun Nanonets.

Author

Hernandez-Padilla, Christian, Joosten, Ben, Van Dries, Koen, and Nain, Amrinder S.

Abstract

Dendritic cells (DCs) are the sentinels of the body responsible for identifying foreign bodies for active defense against invasion. Natively, DCs exist in immature states and quickly mature to migrate faster when detecting signs of foreign invasion. To achieve this unique function, nature has engineered DCs to have high cell motility in 3-dimensional fibrous environments. However, DC cell motility has been extensively studied in flat 2D surfaces, and the impact of the body's fibrous environment, such as matrix porosity and fiber diameter remains poorly described. Using non-electrospinning Spinneret-based Tunable Engineering Parameters (STEP) fiber fabrication platform, we have designed suspended fiber networks that mimic natural fibrous environments to investigate DC migration. First, we designed anisotropic architectures of contrasting diameters (200 and 500nm) that were deposited orthogonally on top of large diameter (~3000nm) fibers and fused at the intersections for fixed/fixed boundary conditions (Figure 1A). We found that immature DCs (iDCs) transitioned from a low (high force) to high (low force and rounded morphology) motility (migratory states) state (Figure 1B). We discovered a remarkable ability of DCs to take cues from the parallel arrangement of fibers to migrate perpendicularly to the direction of fibers through the application of forces using dendritic protrusions (Figure 1C). Since cells were capable of migrating mostly independent of fibrous spacing and alignment it motivated us to extend the studies to the use of crosshatch fiber networks of different diameters (200 and 500nm) with fused nodes. Strikingly, cells in 200nm uniform grids had increased migration paths, while on 500nm crosshatches the migration was reduced. Interestingly, in parallel networks, the effects on the two diameters were not significant, thus, suggesting that fiber architecture enhanced DC migration. We used our previously reported Nanonet Force Microscopy to measure DC migratory forces from the fiber deflections (Figure 1D-E) and found higher forces for non-motile cells (~2.5-8nN). Overall, we emphasize the importance of using fibrous networks of controlled dimensions and architectures to develop new knowledge and understanding of immune cells. [ABSTRACT FROM AUTHOR]

Published
2022

36. The neck region of the C-type lectin DC-SIGN regulates its surface spatiotemporal organization and virus-binding capacity on antigen-presenting cells*

Author

Universitat Politècnica de Catalunya. Departament d'Enginyeria Agroalimentària i Biotecnologia, Manzo, Carlo, Torreño Piña, Juan Andrés, Joosten, Ben, Reinieren Beeren, Inge, Gualda Manzano, Emilio José, Loza Álvarez, Pablo, Figdor, Carl G., Garcia-Parajo, Maria F., Cambi, Alessandra, Universitat Politècnica de Catalunya. Departament d'Enginyeria Agroalimentària i Biotecnologia, Manzo, Carlo, Torreño Piña, Juan Andrés, Joosten, Ben, Reinieren Beeren, Inge, Gualda Manzano, Emilio José, Loza Álvarez, Pablo, Figdor, Carl G., Garcia-Parajo, Maria F., and Cambi, Alessandra

Abstract

The C-type lectin DC-SIGN expressed on dendritic cells(DCs) facilitates capture and internalization of a plethora of dif-ferent pathogens. Although it is known that DC-SIGN organizesin nanoclusters at the surface of DCs, the molecular mecha-nisms responsible for this well defined nanopatterning and rolein viral binding remain enigmatic. By combining biochemicaland advanced biophysical techniques, including optical super-resolution and single particle tracking, we demonstrate thatDC-SIGN intrinsic nanoclustering strictly depends on itsmolecular structure. DC-SIGN nanoclusters exhibited free,Brownian diffusion on the cell membrane, Postprint (published version)

Published
2012

37. The formins FHOD1 and INF2 regulate inter- and intra-structural contractility of podosomes.

Author

Panzer, Linda, Trübe, Leona, Klose, Matthias, Joosten, Ben, Slotman, Johan, Cambi, Alessandra, and Linder, Stefan

Subjects
FORMINS, ACTOMYOSIN, ACTIN, EMBRYOLOGY, CYTOSKELETAL proteins
Abstract

Podosomes are actin-rich adhesion structures that depend on Arp2/3-complex-based actin nucleation. We now report the identification of the formins FHOD1 and INF2 as novel components and additional actin-based regulators of podosomes in primary human macrophages. FHOD1 surrounds the podosome core and is also present at podosome-connecting cables, whereas INF2 localizes at the podosome cap structure. Using a variety of microscopy-based methods; including a semiautomated podosome reformation assay, measurement of podosome oscillations, FRAP analysis of single podosomes, and structured illumination microscopy, both formins were found to regulate different aspects of podosome-associated contractility, with FHOD1 mediating actomyosin contractility between podosomes, and INF2 regulating contractile events at individual podosomes. Moreover, INF2 was found to be a crucial regulator of podosome de novo formation and size. Collectively, we identify FHOD1 and INF2 as novel regulators of inter- and intra-structural contractility of podosomes. Podosomes thus present as one of the few currently identified structures which depend on the concerted activity of both Arp2/3 complex and specific formins and might serve as a model system for the analysis of complex actin architectures in cells. [ABSTRACT FROM AUTHOR]

Published
2016
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