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39 results on '"Boujemaa-Paterski, Rajaa"'

2. Allosteric activation of vinculin by talin

Author

Franz, Florian, Tapia-Rojo, Rafael, Winograd-Katz, Sabina, Boujemaa-Paterski, Rajaa, Li, Wenhong, Unger, Tamar, Albeck, Shira, Aponte-Santamaria, Camilo, Garcia-Manyes, Sergi, Medalia, Ohad, Geiger, Benjamin, and Gräter, Frauke

Published
2023
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8. The Multicellular Effects of VDAC1 N-Terminal-Derived Peptide

Author

Anand, Uttpal, primary, Shteinfer-Kuzmine, Anna, additional, Sela, Gal, additional, Santhanam, Manikandan, additional, Gottschalk, Benjamin, additional, Boujemaa-Paterski, Rajaa, additional, Medalia, Ohad, additional, Graier, Wolfgang F., additional, and Shoshan-Barmatz, Varda, additional

Published
2022
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10. How talin allosterically activates vinculin

Author

Franz, Florian, primary, Tapia-Rojo, Rafael, additional, Katz, Sabina, additional, Boujemaa-Paterski, Rajaa, additional, Li, Wenhong, additional, Unger, Tamar, additional, Albeck, Shira, additional, Aponte-Santamaría, Camilo, additional, Garcia-Manyes, Sergi, additional, Medalia, Ohad, additional, Geiger, Benjamin, additional, and Gräter, Frauke, additional

Published
2022
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14. Directed Actin Assembly and Motility

Author

Boujemaa-Paterski, Rajaa, primary, Galland, Rémi, additional, Suarez, Cristian, additional, Guérin, Christophe, additional, Théry, Manuel, additional, and Blanchoin, Laurent, additional

Published
2014
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15. Talin-activated vinculin interacts with branched actin networks to initiate bundles

Author

Boujemaa-Paterski, Rajaa, Martins, Bruno, Eibauer, Matthias, Beales, Charlie T, Geiger, Benjamin, Medalia, Ohad, and University of Zurich

Subjects
Talin, Electron Microscope Tomography, Integrins, animal structures, QH301-705.5, Science, 610 Medicine & health, macromolecular substances, confocal microscopy, Actin-Related Protein 2-3 Complex, Biochemistry and Chemical Biology, None, 10019 Department of Biochemistry, Cell Adhesion, Sf9 Cells, Animals, Humans, Biology (General), cryo-elecron tomography, Microscopy, Confocal, vinculin, Cryoelectron Microscopy, Actins, Extracellular Matrix, Actin Cytoskeleton, 570 Life sciences, biology, Medicine, actin, Research Article
Abstract

Vinculin plays a fundamental role in integrin-mediated cell adhesion. Activated by talin, it interacts with diverse adhesome components, enabling mechanical coupling between the actin cytoskeleton and the extracellular matrix. Here we studied the interactions of activated full-length vinculin with actin and the way it regulates the organization and dynamics of the Arp2/3 complex-mediated branched actin network. Through a combination of surface patterning and light microscopy experiments we show that vinculin can bundle dendritic actin networks through rapid binding and filament crosslinking. We show that vinculin promotes stable but flexible actin bundles having a mixed-polarity organization, as confirmed by cryo-electron tomography. Adhesion-like synthetic design of vinculin activation by surface-bound talin revealed that clustered vinculin can initiate and immobilize bundles from mobile Arp2/3-branched networks. Our results provide a molecular basis for coordinate actin bundle formation at nascent adhesions.

Published
2020

16. Listeria protein ActA mimics WASP family proteins: it activates filament barbed end branching by Arp2/3 complex

Author

Boujemaa-Paterski, Rajaa, Gouin, Edith, Hansen, Guido, Samarin, Stanislav, Clainche, Christophe Le, Didry, Dominique, Dehoux, Pierre, Cossart, Pascale, Kocks, Christine, Carlier, Marie-France, and Pantaloni, Dominique

Subjects
Binding sites (Biochemistry) -- Analysis, Bacteria -- Motility, Actin -- Physiological aspects, Structure-activity relationships (Biochemistry) -- Analysis, Biological sciences, Chemistry
Abstract

Results demonstrate that the N-terminal domain of ActA binds one actin monomer and the Arp2/3 complex mimicking the C-terminal domain of WASp family proteins. Data show that filament debranching is 3-4-fold faster with ActA activated Arp2/3 that by the C-terminal domain of N-Wasp.

Published
2001

26. Autonomous and in trans functions for the two halves of Srv2/CAP in promoting actin turnover

Author

Chaudhry, Faisal, Jansen, Silvia, Little, Kristin, Suarez, Cristian, Boujemaa-Paterski, Rajaa, Blanchoin, Laurent, Goode, Bruce L., Brandeis University, Rosenstiel Basic Medical Sciences Research Center [Waltham], Laboratoire de physiologie cellulaire végétale (LPCV), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de la Recherche Agronomique (INRA)-Université Joseph Fourier - Grenoble 1 (UJF)-Centre National de la Recherche Scientifique (CNRS), Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Recherche Agronomique (INRA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), and Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Recherche Agronomique (INRA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)

Subjects
Cofilin 1, [SDV.SA]Life Sciences [q-bio]/Agricultural sciences, Actin turnover, Saccharomyces cerevisiae Proteins, [SDV]Life Sciences [q-bio], cytoskeleton, macromolecular substances, cofilin, yeast, Article, Actins, Cytoskeletal Proteins, cyclase-associated protein, Yeasts, Cyclase associated protein, Animals, Rabbits, Carrier Proteins, actin, Adaptor Proteins, Signal Transducing
Abstract

International audience; Recent evidence has suggested that Srv2/CAP (cyclase-associated protein) has two distinct functional roles in regulating actin turnover, with its N-terminus enhancing cofilin-mediated severing of actin filaments and its C-terminus catalyzing actin monomer recycling. However, it has remained unclear to what degree these two activities are coordinated by being linked in one molecule, or whether they can function autonomously. To address this, we physically divided the protein into two separate halves, N-Srv2 and C-Srv2, and asked whether they are able to function in trans both in living cells and in reconstituted assays for F-actin turnover and actin-based motility. Remarkably, in F-actin turnover assays the stimulatory effects of N-Srv2 and C-Srv2 functioning in trans were quantitatively similar to those of intact full-length Srv2. Further, in bead motility assays and in vivo, the fragments again functioned in trans, although not with the full effectiveness of intact Srv2. From these data, we conclude that the functions of the two halves of Srv2/CAP are largely autonomous, although their linkage improves coordination of the two functions in specific settings, possibly explaining why the linkage is conserved across distant plant, animal, and fungal species.

Published
2014

27. Actin network architecture determines myosin motor activity

Author

Reymann, A-C., Boujemaa-Paterski, Rajaa, Martiel, J-L., Cao, W., Chin, H., de La Cruz, E., Thery, M., Blanchoin, Laurent, Institut National de la Recherche Agronomique (INRA), Commissariat à l'énergie atomique et aux énergies alternatives (CEA), Centre National de la Recherche Scientifique (CNRS), Université Joseph Fourier - Grenoble 1 (UJF), Laboratoire de physiologie cellulaire végétale (LPCV), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Joseph Fourier - Grenoble 1 (UJF)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA), Institut de Biosciences et de Biotechnologies de Grenoble (ex-IRTSV) (BIG), Institut National de la Santé et de la Recherche Médicale (INSERM)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Université Joseph Fourier - Grenoble 1 (UJF)-Centre National de la Recherche Scientifique (CNRS)-Institut National de la Recherche Agronomique (INRA)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019]), Yale University [New Haven], Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Recherche Agronomique (INRA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Centre National de la Recherche Scientifique (CNRS)-Institut de Recherche Interdisciplinaire de Grenoble (IRIG), Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA), and Université Joseph Fourier - Grenoble 1 (UJF)-Institut National de la Recherche Agronomique (INRA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS)-Université Grenoble Alpes [2016-2019] (UGA [2016-2019])

Subjects
myosin motors, [SDV]Life Sciences [q-bio], network architecture, ComputingMilieux_MISCELLANEOUS
Abstract

International audience

Published
2011

36. How actin network dynamics control the onset of actin-based motility.

Author

Kawsk, Agnieszka, Carvalho, Kevin, Manzi, John, Boujemaa-Paterski, Rajaa, Blanchoin, Laurent, Martiel, Jean-Louis, and Sykes, Cécile

Subjects
ACTIN, MOLECULAR dynamics, CELL motility, CELLULAR control mechanisms, CELL growth, CELLULAR mechanics
Abstract

Cells use their dynamic actin network to control their mechanics and motility. These networks are made of branched actin filaments generated by the Arp2/3 complex. Here we study under which conditions the microscopic organization of branched actin networks builds up a sufficient stress to trigger sustained motility. In our experimental setup, dynamic actin networks or "gels" are grown on a hard bead in a controlled minimal protein system containing actin monomers, profilin, the Arp2/3 complex and capping protein. We vary protein concentrations and follow experimentally and through simulations the shape and mechanical properties of the actin gel growing around beads. Actin gel morphology is controlled by elementary steps including "primer" contact, growth of the network, entanglement, mechanical interaction and force production. We show that varying the biochemical orchestration of these steps can lead to the loss of network cohesion and the lack of effective force production. We propose a predictive phase diagram of actin gel fate as a function of protein concentrations. This work unveils how, in growing actin networks, a tight biochemical and physical coupling smoothens initial primer-caused heterogeneities and governs force buildup and cell motility. [ABSTRACT FROM AUTHOR]

Published
2012
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37. Keratin isoform shifts modulate motility signals during wound healing.

Author

Nanes BA, Bhatt K, Boujemaa-Paterski R, Azarova E, Munawar S, Rajendran D, Isogai T, Dean KM, Medalia O, and Danuser G

Abstract

Keratin intermediate filaments form strong mechanical scaffolds that confer structural stability to epithelial tissues, but the reason this function requires a protein family with 54 isoforms is not understood. During skin wound healing, a shift in keratin isoform expression alters the composition of keratin filaments. How this change modulates cellular function to support epidermal remodeling remains unclear. We report an unexpected effect of keratin isoform variation on kinase signal transduction. Increased expression of wound-associated keratin 6A, but not of steady-state keratin 5, potentiated keratinocyte migration and wound closure without compromising epidermal stability by activating myosin motors. This pathway depended on isoform-specific interaction between intrinsically disordered keratin head domains and non-filamentous vimentin shuttling myosin-activating kinases. These results substantially expand the functional repertoire of intermediate filaments from their canonical role as mechanical scaffolds to include roles as isoform-tuned signaling scaffolds that organize signal transduction cascades in space and time to influence epithelial cell state.

Published
2024
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38. Autonomous and in trans functions for the two halves of Srv2/CAP in promoting actin turnover.

Author

Chaudhry F, Jansen S, Little K, Suarez C, Boujemaa-Paterski R, Blanchoin L, and Goode BL

Subjects
Animals, Rabbits, Yeasts, Actins metabolism, Adaptor Proteins, Signal Transducing metabolism, Carrier Proteins metabolism, Cofilin 1 metabolism, Cytoskeletal Proteins metabolism, Saccharomyces cerevisiae Proteins metabolism
Abstract

Recent evidence has suggested that Srv2/CAP (cyclase-associated protein) has two distinct functional roles in regulating actin turnover, with its N-terminus enhancing cofilin-mediated severing of actin filaments and its C-terminus catalyzing actin monomer recycling. However, it has remained unclear to what degree these two activities are coordinated by being linked in one molecule, or whether they can function autonomously. To address this, we physically divided the protein into two separate halves, N-Srv2 and C-Srv2, and asked whether they are able to function in trans both in living cells and in reconstituted assays for F-actin turnover and actin-based motility. Remarkably, in F-actin turnover assays the stimulatory effects of N-Srv2 and C-Srv2 functioning in trans were quantitatively similar to those of intact full-length Srv2. Further, in bead motility assays and in vivo, the fragments again functioned in trans, although not with the full effectiveness of intact Srv2. From these data, we conclude that the functions of the two halves of Srv2/CAP are largely autonomous, although their linkage improves coordination of the two functions in specific settings, possibly explaining why the linkage is conserved across distant plant, animal, and fungal species., (© 2014 Wiley Periodicals, Inc.)

Published
2014
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39. Directed actin assembly and motility.

Author

Boujemaa-Paterski R, Galland R, Suarez C, Guérin C, Théry M, and Blanchoin L

Subjects
Actin Cytoskeleton chemistry, Actins chemistry, Animals, Equipment Design, Lasers, Microfluidic Analytical Techniques instrumentation, Microfluidic Analytical Techniques methods, Microscopy, Fluorescence instrumentation, Microscopy, Fluorescence methods, Polymerization, Ultraviolet Rays, Actin Cytoskeleton metabolism, Actin Cytoskeleton ultrastructure, Actins metabolism, Actins ultrastructure
Abstract

The actin cytoskeleton is a key component of the cellular architecture. However, understanding actin organization and dynamics in vivo is a complex challenge. Reconstitution of actin structures in vitro, in simplified media, allows one to pinpoint the cellular biochemical components and their molecular interactions underlying the architecture and dynamics of the actin network. Previously, little was known about the extent to which geometrical constraints influence the dynamic ultrastructure of these networks. Therefore, in order to study the balance between biochemical and geometrical control of complex actin organization, we used the innovative methodologies of UV and laser patterning to design a wide repertoire of nucleation geometries from which we assembled branched actin networks. Using these methods, we were able to reconstitute complex actin network organizations, closely related to cellular architecture, to precisely direct and control their 3D connections. This methodology mimics the actin networks encountered in cells and can serve in the fabrication of innovative bioinspired systems., (© 2014 Elsevier Inc. All rights reserved.)

Published
2014
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