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Article ; Online: Integrin Facilitates the Internalization of TAT Peptide Conjugated to RGD Motif in Model Lipid Membranes.

Ciobanasu, Corina / Pernier, Julien / Le Clainche, Christophe

Chembiochem : a European journal of chemical biology

2023 Volume 25, Issue 2, Page(s) e202300642

Abstract: In recent years, targeted drug delivery has attracted a great interest for enhanced therapeutic efficiency, with diminished side effects, especially in cancer therapy. Cell penetrating peptides (CPPs) like HIV1-TAT peptides, appear to be the perfect ... ...

Abstract	In recent years, targeted drug delivery has attracted a great interest for enhanced therapeutic efficiency, with diminished side effects, especially in cancer therapy. Cell penetrating peptides (CPPs) like HIV1-TAT peptides, appear to be the perfect vectors for translocating drugs or other cargoes across the plasma membrane, but their application is limited mostly due to insufficient specificity for intended targets. Although these molecules were successfully used, the mechanism by which the peptides enter the cell interior still needs to be clarified. The tripeptide motif RGD (arginine-glycine-aspartate), found in extracellular matrix proteins has high affinity for integrin receptors overexpressed in cancer and it is involved in different phases of disease progression, including proliferation, invasion and migration. Discovery of new peptides with high binding affinity for disease receptors and permeability of plasma membranes is desirable for both, development of targeted drug delivery systems and early detection and diagnosis. To complement the TAT peptide with specific targeting ability, we conjugated it with an integrin-binding RGD motif. Although the idea of RGD-CPPs conjugates is not entirely new,
MeSH term(s)	Humans ; Integrins/metabolism ; Oligopeptides/chemistry ; Cell-Penetrating Peptides/chemistry ; Neoplasms ; Lipids
Chemical Substances	Integrins ; Oligopeptides ; Cell-Penetrating Peptides ; Lipids
Language	English
Publishing date	2023-11-23
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2020469-3
ISSN	1439-7633 ; 1439-4227
ISSN (online)	1439-7633
ISSN	1439-4227
DOI	10.1002/cbic.202300642
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Article ; Online: Talin dissociates from RIAM and associates to vinculin sequentially in response to the actomyosin force.

Vigouroux, Clémence / Henriot, Véronique / Le Clainche, Christophe

Nature communications

2020 Volume 11, Issue 1, Page(s) 3116

Abstract: Cells reinforce adhesion strength and cytoskeleton anchoring in response to the actomyosin force. The mechanical stretching of talin, which exposes cryptic vinculin-binding sites, triggers this process. The binding of RIAM to talin could regulate this ... ...

Abstract	Cells reinforce adhesion strength and cytoskeleton anchoring in response to the actomyosin force. The mechanical stretching of talin, which exposes cryptic vinculin-binding sites, triggers this process. The binding of RIAM to talin could regulate this mechanism. However, the mechanosensitivity of the talin-RIAM complex has never been tested. It is also not known whether RIAM controls the mechanosensitivity of the talin-vinculin complex. To address these issues, we designed an in vitro microscopy assay with purified proteins in which the actomyosin force controls RIAM and vinculin-binding to talin. We demonstrate that actomyosin triggers RIAM dissociation from several talin domains. Actomyosin also provokes the sequential exchange of RIAM for vinculin on talin. The effect of RIAM on this force-dependent binding of vinculin to talin varies from one talin domain to another. This mechanism could allow talin to biochemically code a wide range of forces by selecting different combinations of partners.
MeSH term(s)	Actomyosin/isolation & purification ; Actomyosin/metabolism ; Adaptor Proteins, Signal Transducing/genetics ; Adaptor Proteins, Signal Transducing/isolation & purification ; Adaptor Proteins, Signal Transducing/metabolism ; Animals ; Genes, Reporter/genetics ; Luminescent Proteins/genetics ; Membrane Proteins/genetics ; Membrane Proteins/isolation & purification ; Membrane Proteins/metabolism ; Microscopy, Fluorescence ; Molecular Imaging ; Muscle, Skeletal ; Rabbits ; Recombinant Proteins/genetics ; Recombinant Proteins/isolation & purification ; Recombinant Proteins/metabolism ; Talin/genetics ; Talin/isolation & purification ; Talin/metabolism ; Vinculin/genetics ; Vinculin/isolation & purification ; Vinculin/metabolism
Chemical Substances	APBB1IP protein, human ; Adaptor Proteins, Signal Transducing ; Luminescent Proteins ; Membrane Proteins ; Recombinant Proteins ; TLN1 protein, human ; Talin ; VCL protein, human ; Vinculin (125361-02-6) ; Actomyosin (9013-26-7)
Language	English
Publishing date	2020-06-19
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Video-Audio Media
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-020-16922-1
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Article ; Online: Actin polymerization downstream of integrins: signaling pathways and mechanotransduction.

Romero, Stéphane / Le Clainche, Christophe / Gautreau, Alexis M

The Biochemical journal

2020 Volume 477, Issue 1, Page(s) 1–21

Abstract: A cell constantly adapts to its environment. Cell decisions to survive, to proliferate or to migrate are dictated not only by soluble growth factors, but also through the direct interaction of the cell with the surrounding extracellular matrix (ECM). ... ...

Abstract	A cell constantly adapts to its environment. Cell decisions to survive, to proliferate or to migrate are dictated not only by soluble growth factors, but also through the direct interaction of the cell with the surrounding extracellular matrix (ECM). Integrins and their connections to the actin cytoskeleton are crucial for monitoring cell attachment and the physical properties of the substratum. Cell adhesion dynamics are modulated in complex ways by the polymerization of branched and linear actin arrays, which in turn reinforce ECM-cytoskeleton connection. This review describes the major actin regulators, Ena/VASP proteins, formins and Arp2/3 complexes, in the context of signaling pathways downstream of integrins. We focus on the specific signaling pathways that transduce the rigidity of the substrate and which control durotaxis, i.e. directed migration of cells towards increased ECM rigidity. By doing so, we highlight several recent findings on mechanotransduction and put them into a broad integrative perspective that is the result of decades of intense research on the actin cytoskeleton and its regulation.
MeSH term(s)	Actin-Related Protein 2-3 Complex/metabolism ; Actins/metabolism ; Animals ; Cell Adhesion ; DNA-Binding Proteins/metabolism ; Extracellular Matrix/metabolism ; Formins/metabolism ; Humans ; Integrins/metabolism ; Mechanotransduction, Cellular ; Mice ; Polymerization
Chemical Substances	Actin-Related Protein 2-3 Complex ; Actins ; DNA-Binding Proteins ; ENA-VASP proteins ; Formins ; Integrins
Language	English
Publishing date	2020-01-08
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ZDB-ID	2969-5
ISSN	1470-8728 ; 0006-2936 ; 0306-3275 ; 0264-6021
ISSN (online)	1470-8728
ISSN	0006-2936 ; 0306-3275 ; 0264-6021
DOI	10.1042/BCJ20170719
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Article ; Online: Impulse oscillometry indices to detect an abnormal lung clearance index in childhood cystic fibrosis.

Bokov, Plamen / Gerardin, Michele / Le Clainche, Laurence / Houdouin, Véronique / Delclaux, Christophe

Pediatric pulmonology

2021 Volume 56, Issue 12, Page(s) 3752–3757

Abstract: The objective of our cross-sectional study was to assess the relationships between indices of multiple breath washout (MBW) and impulse oscillometry system (IOS) in cystic fibrosis in forty consecutive children (median age 8.1 years) in stable conditions ...

Abstract	The objective of our cross-sectional study was to assess the relationships between indices of multiple breath washout (MBW) and impulse oscillometry system (IOS) in cystic fibrosis in forty consecutive children (median age 8.1 years) in stable conditions and to evaluate whether cut-off values of IOS indices may help to avoid MBW, which is time-consuming. IOS measurements took a median duration of 3 min, while MBW measurements took a median duration of 49 min. Lung Clearance Index (LCI
MeSH term(s)	Child ; Cross-Sectional Studies ; Cystic Fibrosis/diagnosis ; Forced Expiratory Volume ; Humans ; Lung ; Oscillometry ; Spirometry
Language	English
Publishing date	2021-09-02
Publishing country	United States
Document type	Journal Article
ZDB-ID	632784-9
ISSN	1099-0496 ; 8755-6863
ISSN (online)	1099-0496
ISSN	8755-6863
DOI	10.1002/ppul.25649
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Article ; Online: Talin dissociates from RIAM and associates to vinculin sequentially in response to the actomyosin force

Clémence Vigouroux / Véronique Henriot / Christophe Le Clainche

Nature Communications, Vol 11, Iss 1, Pp 1-

2020 Volume 11

Abstract: Force-dependent formation of the talin-vinculin complex reinforces actin anchoring to focal adhesions, but how different talin-binding proteins respond to force is unclear. Here authors use an in vitro microscopy assay and show that the actomyosin force ... ...

Abstract	Force-dependent formation of the talin-vinculin complex reinforces actin anchoring to focal adhesions, but how different talin-binding proteins respond to force is unclear. Here authors use an in vitro microscopy assay and show that the actomyosin force triggers the dissociation of RIAM from several talin domains.
Keywords	Science ; Q
Language	English
Publishing date	2020-06-01T00:00:00Z
Publisher	Nature Portfolio
Document type	Article ; Online
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Article ; Online: Talin and kindlin cooperate to control the density of integrin clusters.

Pernier, Julien / Cardoso Dos Santos, Marcelina / Souissi, Mariem / Joly, Adrien / Narassimprakash, Hemalatha / Rossier, Olivier / Giannone, Grégory / Helfer, Emmanuèle / Sengupta, Kheya / Le Clainche, Christophe

Journal of cell science

2023 Volume 136, Issue 8

Abstract: Focal adhesions are composed of transmembrane integrins, linking the extracellular matrix to the actomyosin cytoskeleton, via cytoplasmic proteins. Adhesion depends on the activation of integrins. Talin and kindlin proteins are intracellular activators ... ...

Abstract	Focal adhesions are composed of transmembrane integrins, linking the extracellular matrix to the actomyosin cytoskeleton, via cytoplasmic proteins. Adhesion depends on the activation of integrins. Talin and kindlin proteins are intracellular activators of integrins that bind to β-integrin cytoplasmic tails. Integrin activation and clustering through extracellular ligands guide the organization of adhesion complexes. However, the roles of talin and kindlin in this process are poorly understood. To determine the contribution of talin, kindlin, lipids and actomyosin in integrin clustering, we used a biomimetic in vitro system, made of giant unilamellar vesicles, containing transmembrane integrins (herein αIIbβ3), with purified talin (talin-1), kindlin (kindlin-2, also known as FERMT2) and actomyosin. Here, we show that talin and kindlin individually have the ability to cluster integrins. Talin and kindlin synergize to induce the formation of larger integrin clusters containing the three proteins. Comparison of protein density reveals that kindlin increases talin and integrin density, whereas talin does not affect kindlin and integrin density. Finally, kindlin increases integrin-talin-actomyosin coupling. Our study unambiguously demonstrates how kindlin and talin cooperate to induce integrin clustering, which is a major parameter for cell adhesion.
MeSH term(s)	Integrins/metabolism ; Talin/genetics ; Talin/metabolism ; Actomyosin ; Membrane Proteins/metabolism ; Neoplasm Proteins/genetics ; Neoplasm Proteins/metabolism ; Platelet Glycoprotein GPIIb-IIIa Complex/metabolism ; Cell Adhesion
Chemical Substances	Integrins ; Talin ; Actomyosin (9013-26-7) ; Membrane Proteins ; Neoplasm Proteins ; Platelet Glycoprotein GPIIb-IIIa Complex
Language	English
Publishing date	2023-04-21
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
DOI	10.1242/jcs.260746
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Zs.A 1200: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
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Article ; Online: Integrin-Functionalised Giant Unilamellar Vesicles via Gel-Assisted Formation: Good Practices and Pitfalls.

Souissi, Mariem / Pernier, Julien / Rossier, Olivier / Giannone, Gregory / Le Clainche, Christophe / Helfer, Emmanuèle / Sengupta, Kheya

International journal of molecular sciences

2021 Volume 22, Issue 12

Abstract: Giant unilamellar vesicles (GUV) are powerful tools to explore physics and biochemistry of the cell membrane in controlled conditions. For example, GUVs were extensively used to probe cell adhesion, but often using non-physiological linkers, due to the ... ...

Abstract	Giant unilamellar vesicles (GUV) are powerful tools to explore physics and biochemistry of the cell membrane in controlled conditions. For example, GUVs were extensively used to probe cell adhesion, but often using non-physiological linkers, due to the difficulty of incorporating transmembrane adhesion proteins into model membranes. Here we describe a new protocol for making GUVs incorporating the transmembrane protein integrin using gel-assisted swelling. We report an optimised protocol, enumerating the pitfalls encountered and precautions to be taken to maintain the robustness of the protocol. We characterise intermediate steps of small proteoliposome formation and the final formed GUVs. We show that the integrin molecules are successfully incorporated and are functional.
MeSH term(s)	Cell Adhesion ; Fluorescence ; Gels/chemistry ; Humans ; Integrins/metabolism ; Lipid Bilayers/metabolism ; Lipids/chemistry ; Particle Size ; Unilamellar Liposomes/chemistry
Chemical Substances	Gels ; Integrins ; Lipid Bilayers ; Lipids ; Unilamellar Liposomes
Language	English
Publishing date	2021-06-13
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms22126335
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Article ; Online: Activated I-BAR IRSp53 clustering controls the formation of VASP-actin-based membrane protrusions.

Tsai, Feng-Ching / Henderson, J Michael / Jarin, Zack / Kremneva, Elena / Senju, Yosuke / Pernier, Julien / Mikhajlov, Oleg / Manzi, John / Kogan, Konstantin / Le Clainche, Christophe / Voth, Gregory A / Lappalainen, Pekka / Bassereau, Patricia

Science advances

2022 Volume 8, Issue 41, Page(s) eabp8677

Abstract: Filopodia are actin-rich membrane protrusions essential for cell morphogenesis, motility, and cancer invasion. How cells control filopodium initiation on the plasma membrane remains elusive. We performed experiments in cellulo, in vitro, and in silico to ...

Abstract	Filopodia are actin-rich membrane protrusions essential for cell morphogenesis, motility, and cancer invasion. How cells control filopodium initiation on the plasma membrane remains elusive. We performed experiments in cellulo, in vitro, and in silico to unravel the mechanism of filopodium initiation driven by the membrane curvature sensor IRSp53 (insulin receptor substrate protein of 53 kDa). We showed that full-length IRSp53 self-assembles into clusters on membranes depending on PIP
Language	English
Publishing date	2022-10-14
Publishing country	United States
Document type	Journal Article
ZDB-ID	2810933-8
ISSN	2375-2548 ; 2375-2548
ISSN (online)	2375-2548
ISSN	2375-2548
DOI	10.1126/sciadv.abp8677
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Article ; Online: Direct measurement of near-nano-Newton forces developed by self-organizing actomyosin fibers bound α-catenin.

Sonam, Surabhi / Vigouroux, Clémence / Jégou, Antoine / Romet-Lemonne, Guillaume / Le Clainche, Christophe / Ladoux, Benoit / Mège, René Marc

Biology of the cell

2021 Volume 113, Issue 11, Page(s) 441–449

Abstract: Background information: Actin cytoskeleton contractility plays a critical role in morphogenetic processes by generating forces that are then transmitted to cell-cell and cell-ECM adhesion complexes. In turn, mechanical properties of the environment are ... ...

Abstract	Background information: Actin cytoskeleton contractility plays a critical role in morphogenetic processes by generating forces that are then transmitted to cell-cell and cell-ECM adhesion complexes. In turn, mechanical properties of the environment are sensed and transmitted to the cytoskeleton at cell adhesion sites, influencing cellular processes such as cell migration, differentiation and survival. Anchoring of the actomyosin cytoskeleton to adhesion sites is mediated by adaptor proteins such as talin or α-catenin that link F-actin to transmembrane cell adhesion receptors, thereby allowing mechanical coupling between the intracellular and extracellular compartments. Thus, a key issue is to be able to measure the forces generated by actomyosin and transmitted to the adhesion complexes. Approaches developed in cells and those probing single molecule mechanical properties of α-catenin molecules allowed to identify α-catenin, an F-actin binding protein which binds to the cadherin complexes as a major player in cadherin-based mechanotransduction. However, it is still very difficult to bridge intercellular forces measured at cellular levels and those measured at the single-molecule level. Results: Here, we applied an intermediate approach allowing reconstruction of the actomyosin-α-catenin complex in acellular conditions to probe directly the transmitted forces. For this, we combined micropatterning of purified α-catenin and spontaneous actomyosin network assembly in the presence of G-actin and Myosin II with microforce sensor arrays used so far to measure cell-generated forces. Conclusions: Using this method, we show that self-organizing actomyosin bundles bound to micrometric α-catenin patches can apply near-nano-Newton forces. Significance: Our results pave the way for future studies on molecular/cellular mechanotransduction and mechanosensing.
MeSH term(s)	Actin Cytoskeleton/metabolism ; Actins/metabolism ; Actomyosin/metabolism ; Cadherins ; Cell Adhesion ; Mechanotransduction, Cellular ; alpha Catenin/metabolism
Chemical Substances	Actins ; Cadherins ; alpha Catenin ; Actomyosin (9013-26-7)
Language	English
Publishing date	2021-08-20
Publishing country	England
Document type	Journal Article
ZDB-ID	245745-3
ISSN	1768-322X ; 0399-0311 ; 0248-4900
ISSN (online)	1768-322X
ISSN	0399-0311 ; 0248-4900
DOI	10.1111/boc.202100014
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Zs.A 758: Show issues

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Article ; Online: Beneficial short-term effect of autogenic drainage on peripheral resistance in childhood cystic fibrosis disease.

Bokov, Plamen / Gerardin, Michèle / Brialix, Géraldine / Da Costa Noble, Emmanuelle / Juif, Romain / Foucher, Antonia Vital / Le Clainche, Laurence / Houdouin, Véronique / Mauroy, Benjamin / Delclaux, Christophe

BMC pulmonary medicine

2022 Volume 22, Issue 1, Page(s) 241

Abstract: Background: Airway clearance techniques are supposed to be a necessary adjunct for the enhancement of impaired peripheral clearance in cystic fibrosis (CF). The objective was to assess the effect of one physiotherapy session (autogenic drainage: AD) on ... ...

Abstract	Background: Airway clearance techniques are supposed to be a necessary adjunct for the enhancement of impaired peripheral clearance in cystic fibrosis (CF). The objective was to assess the effect of one physiotherapy session (autogenic drainage: AD) on mucus clearance (sputum wet weight) and impulse oscillometry system (IOS) indices, including those obtained from extended Resistance-Inertance-Compliance (eRIC) modelling, considering the degree of bronchial congestion. Methods: Thirty children with CF (median age: 12.7 years) in a stable condition prospectively underwent IOS measurements at baseline and after AD. They were divided in two groups: with (visual analog scale of bronchial congestion by the physiotherapist ≥ 5/10) and without (scale < 5/10) bronchial congestion. Paired-comparison of the effects of AD on airway resistance measurements was done with Wilcoxon test. Results: The congestion scale correlated with the wet weight of sputum production during the session (Pearson test: p < 0.0001, R = 0.66). Ten children had bronchial congestion and 20 were without congestion. In the whole group, R5-20 Hz significantly decreased after AD (P = 0.049), which was related to a decrease in the children with congestion (P = 0.025), whereas it was not significantly modified in the children without congestion (P = 0.327). The eRIC model allowed the calculation of the peripheral resistance of the respiratory system, which also decreased in the children with congestion (P = 0.037), however, not modified in the children without congestion (P = 0.390). Conclusion: One session of autogenic drainage has the ability to decrease peripheral resistance obtained from IOS measurements, more specifically in children with CF with moderate to severe bronchial congestion. Trial registration: ClinicalTrials.gov Identifier: NCT04094441.
MeSH term(s)	Child ; Cystic Fibrosis/therapy ; Drainage ; Humans ; Physical Therapy Modalities ; Respiratory Therapy/methods ; Vascular Resistance
Language	English
Publishing date	2022-06-21
Publishing country	England
Document type	Journal Article
ZDB-ID	2059871-3
ISSN	1471-2466 ; 1471-2466
ISSN (online)	1471-2466
ISSN	1471-2466
DOI	10.1186/s12890-022-02039-2
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