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Article: Molecular regulation of cytoskeletal rearrangements during T cell signalling.

Stradal, Theresia E B / Pusch, Rico / Kliche, Stefanie

Results and problems in cell differentiation

2006 Volume 43, Page(s) 219–244

Abstract: ... This is particularly true for the many types of T cells, which are at the foundation of the adaptive ... dynamics are required for proper signal transmission in many processes such as T cell activation ...

Abstract	Regulation of the cytoskeleton in cells of the haematopoietic system is essential for fulfilling diverse tasks such as migration towards a chemoattractant, phagocytosis or cell-cell communication. This is particularly true for the many types of T cells, which are at the foundation of the adaptive immune system in vertebrates. Deregulation of actin filament turnover is known to be involved in the development of severe immunodeficiencies or immunoproliferative diseases. Therefore, molecular dissection of signalling complexes and effector molecules, which leads to controlled cytoskeletal assembly, has been the focus of immunological research in the last decade. In the past, cytoskeletal remodelling was frequently understood as the finish line of signalling, while today it becomes increasingly evident that actin and microtubule dynamics are required for proper signal transmission in many processes such as T cell activation. Significant effort is made in many laboratories to further elucidate the contribution of cytoskeletal remodelling to immune function. The objective of this article is to summarise the current knowledge on how actin and microtubules are reorganised to support the formation of structures as diverse as the immunological synapse and peripheral protrusions during cell migration.
MeSH term(s)	Actin Cytoskeleton/metabolism ; Actins/metabolism ; Animals ; CD28 Antigens/metabolism ; Cytoskeleton/immunology ; Cytoskeleton/metabolism ; Forecasting ; Humans ; Microtubules/metabolism ; Models, Immunological ; Receptors, Antigen, T-Cell/metabolism ; Signal Transduction/immunology ; T-Lymphocytes/cytology ; T-Lymphocytes/immunology ; Tubulin/metabolism
Chemical Substances	Actins ; CD28 Antigens ; Receptors, Antigen, T-Cell ; Tubulin
Language	English
Publishing date	2006-10-26
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Review
ISSN	0080-1844
ISSN	0080-1844
DOI	10.1007/400_022
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Article: Enhancing pre-clinical research with simplified intestinal cell line models.

Fey, Christina / Truschel, Theresa / Nehlsen, Kristina / Damigos, Spyridon / Horstmann, Julia / Stradal, Theresia / May, Tobias / Metzger, Marco / Zdzieblo, Daniela

Journal of tissue engineering

2024 Volume 15, Page(s) 20417314241228949

Abstract: Two-dimensional culture remains widely employed to determine the bioavailability of orally delivered drugs. To gain more knowledge about drug uptake mechanisms and risk assessment for the patient after oral drug admission, intestinal in vitro models ... ...

Abstract	Two-dimensional culture remains widely employed to determine the bioavailability of orally delivered drugs. To gain more knowledge about drug uptake mechanisms and risk assessment for the patient after oral drug admission, intestinal in vitro models demonstrating a closer similarity to the in vivo situation are needed. In particular, Caco-2 cell-based Transwell® models show advantages as they are reproducible, cost-efficient, and standardized. However, cellular complexity is impaired and cell function is strongly modified as important transporters in the apical membrane are missing. To overcome these limitations, primary organoid-based human small intestinal tissue models were developed recently but the application of these cultures in pre-clinical research still represents an enormous challenge, as culture setup is complex as well as time- and cost-intensive. To overcome these hurdles, we demonstrate the establishment of primary organoid-derived intestinal cell lines by immortalization. Besides exhibiting cellular diversity of the organoid, these immortalized cell lines enable a standardized and more cost-efficient culture. Further, our cell line-based Transwell®-like models display an organ-specific epithelial barrier integrity, ultrastructural features and representative transport functions. Altogether, our novel model systems are cost-efficient with close similarity to the in vivo situation, therefore favoring their use in bioavailability studies in the context of pre-clinical screenings.
Language	English
Publishing date	2024-03-04
Publishing country	England
Document type	Journal Article
ZDB-ID	2573915-3
ISSN	2041-7314
ISSN	2041-7314
DOI	10.1177/20417314241228949
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Article: RIAM links the ADAP/SKAP-55 signaling module to Rap1, facilitating T-cell-receptor-mediated integrin activation.

Ménasché, Gaël / Kliche, Stefanie / Chen, Emily J H / Stradal, Theresia E B / Schraven, Burkhart / Koretzky, Gary

Molecular and cellular biology

2007 Volume 27, Issue 11, Page(s) 4070–4081

Abstract: One outcome of T-cell receptor (TCR) signaling is increased affinity and avidity of integrins ... with SKAP-55 in both a heterologous transfection system and primary T cells and map the region essential ... and for efficient conjugate formation between T cells and antigen-presenting cells. Mechanistic ...

Abstract	One outcome of T-cell receptor (TCR) signaling is increased affinity and avidity of integrins for their ligands. This occurs through a process known as inside-out signaling, which has been shown to require several molecular components including the adapter proteins ADAP (adhesion and degranulation-promoting adapter protein) and SKAP-55 (55-kDa src kinase-associated phosphoprotein) and the small GTPase Rap1. Herein, we provide evidence linking ADAP and SKAP-55 to RIAM, a recently described adapter protein that binds selectively to active Rap1. We identified RIAM as a key component linking the ADAP/SKAP-55 module to the small GTPase Rap1, facilitating TCR-mediated integrin activation. We show that RIAM constitutively interacts with SKAP-55 in both a heterologous transfection system and primary T cells and map the region essential for this interaction. Additionally, we find that the SKAP-55/RIAM complex is essential both for TCR-mediated adhesion and for efficient conjugate formation between T cells and antigen-presenting cells. Mechanistic studies revealed that the ADAP/SKAP-55 module relocalized RIAM and Rap1 to the plasma membrane following TCR activation to facilitate integrin activation. These results describe for the first time a link between ADAP/SKAP-55 and the Rap1/RIAM complex and provide a potential new mechanism for TCR-mediated integrin activation.
MeSH term(s)	Adaptor Proteins, Signal Transducing/genetics ; Adaptor Proteins, Signal Transducing/metabolism ; Animals ; Cell Adhesion/physiology ; Cell Line ; Humans ; Integrins/genetics ; Integrins/metabolism ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Mice ; Phosphoproteins/genetics ; Phosphoproteins/metabolism ; Protein Binding ; Receptors, Antigen, T-Cell/genetics ; Receptors, Antigen, T-Cell/metabolism ; Recombinant Fusion Proteins/genetics ; Recombinant Fusion Proteins/metabolism ; Signal Transduction/physiology ; T-Lymphocytes/physiology ; rap1 GTP-Binding Proteins/genetics ; rap1 GTP-Binding Proteins/metabolism
Chemical Substances	Adaptor Proteins, Signal Transducing ; Fyb protein, mouse ; Integrins ; Membrane Proteins ; Phosphoproteins ; RIAM protein, mouse ; Receptors, Antigen, T-Cell ; Recombinant Fusion Proteins ; SKAP55 protein, mouse ; rap1 GTP-Binding Proteins (EC 3.6.5.2)
Language	English
Publishing date	2007-06
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	779397-2
ISSN	1098-5549 ; 0270-7306
ISSN (online)	1098-5549
ISSN	0270-7306
DOI	10.1128/MCB.02011-06
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Article ; Online: Src homology 2-domain containing leukocyte-specific phosphoprotein of 76 kDa is mandatory for TCR-mediated inside-out signaling, but dispensable for CXCR4-mediated LFA-1 activation, adhesion, and migration of T cells.

Horn, Jessica / Wang, Xiaoqian / Reichardt, Peter / Stradal, Theresia E / Warnecke, Nicole / Simeoni, Luca / Gunzer, Matthias / Yablonski, Deborah / Schraven, Burkhart / Kliche, Stefanie

Journal of immunology (Baltimore, Md. : 1950)

2009 Volume 183, Issue 9, Page(s) 5756–5767

Abstract: ... of T cells via so-called inside-out signaling pathways. The molecular processes underlying inside-out ... leukocyte-specific phosphoprotein of 76 kDa (SLP76) is crucial for TCR-mediated inside-out signaling and T ... signaling. Indeed, both CXCR4-induced T cell adhesion and migration are not affected by loss of SLP76 ...

Abstract	Engagement of the TCR or of chemokine receptors such as CXCR4 induces adhesion and migration of T cells via so-called inside-out signaling pathways. The molecular processes underlying inside-out signaling events are as yet not completely understood. In this study, we show that TCR- and CXCR4-mediated activation of integrins critically depends on the membrane recruitment of the adhesion- and degranulation-promoting adapter protein (ADAP)/Src kinase-associated phosphoprotein of 55 kDa (SKAP55)/Rap1-interacting adapter protein (RIAM)/Rap1 module. We further demonstrate that the Src homology 2 domain containing leukocyte-specific phosphoprotein of 76 kDa (SLP76) is crucial for TCR-mediated inside-out signaling and T cell/APC interaction. Besides facilitating membrane recruitment of ADAP, SKAP55, and RIAM, SLP76 regulates TCR-mediated inside-out signaling by controlling the activation of Rap1 as well as Rac-mediated actin polymerization. Surprisingly, however, SLP76 is not mandatory for CXCR4-mediated inside-out signaling. Indeed, both CXCR4-induced T cell adhesion and migration are not affected by loss of SLP76. Moreover, after CXCR4 stimulation, the ADAP/SKAP55/RIAM/Rap1 module is recruited to the plasma membrane independently of SLP76. Collectively, our data indicate a differential requirement for SLP76 in TCR- vs CXCR4-mediated inside-out signaling pathways regulating T cell adhesion and migration.
MeSH term(s)	Adaptor Proteins, Signal Transducing/deficiency ; Adaptor Proteins, Signal Transducing/genetics ; Adaptor Proteins, Signal Transducing/physiology ; Cell Adhesion/genetics ; Cell Adhesion/immunology ; Cells, Cultured ; Chemokine CXCL12/physiology ; Chemotaxis, Leukocyte/genetics ; Chemotaxis, Leukocyte/immunology ; Humans ; Jurkat Cells ; Lymphocyte Activation/genetics ; Lymphocyte Activation/immunology ; Lymphocyte Function-Associated Antigen-1/physiology ; Phosphoproteins/deficiency ; Phosphoproteins/genetics ; Phosphoproteins/physiology ; Receptors, CXCR4/physiology ; Signal Transduction/genetics ; Signal Transduction/immunology ; T-Lymphocyte Subsets/cytology ; T-Lymphocyte Subsets/immunology ; T-Lymphocyte Subsets/metabolism ; Toll-Like Receptors/physiology
Chemical Substances	Adaptor Proteins, Signal Transducing ; CXCL12 protein, human ; CXCR4 protein, human ; Chemokine CXCL12 ; Lymphocyte Function-Associated Antigen-1 ; Phosphoproteins ; Receptors, CXCR4 ; SLP-76 signal Transducing adaptor proteins ; Toll-Like Receptors
Language	English
Publishing date	2009-11-01
Publishing country	United States
Document type	Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	3056-9
ISSN	1550-6606 ; 0022-1767 ; 1048-3233 ; 1047-7381
ISSN (online)	1550-6606
ISSN	0022-1767 ; 1048-3233 ; 1047-7381
DOI	10.4049/jimmunol.0900649
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Article ; Online: Enhancing pre-clinical research with simplified intestinal cell line models

Fey, Christina / Truschel, Theresa / Nehlsen, Kristina / Damigos, Spyridon / Horstmann, Julia / Stradal, Theresia / May, Tobias / Metzger, Marco / Zdzieblo, Daniela

2024

Abstract	Two-dimensional culture remains widely employed to determine the bioavailability of orally delivered drugs. To gain more knowledge about drug uptake mechanisms and risk assessment for the patient after oral drug admission, intestinal in vitro models demonstrating a closer similarity to the in vivo situation are needed. In particular, Caco-2 cell-based Transwell® models show advantages as they are reproducible, cost-efficient, and standardized. However, cellular complexity is impaired and cell function is strongly modified as important transporters in the apical membrane are missing. To overcome these limitations, primary organoid-based human small intestinal tissue models were developed recently but the application of these cultures in pre-clinical research still represents an enormous challenge, as culture setup is complex as well as time- and cost-intensive. To overcome these hurdles, we demonstrate the establishment of primary organoid-derived intestinal cell lines by immortalization. Besides exhibiting cellular diversity of the organoid, these immortalized cell lines enable a standardized and more cost-efficient culture. Further, our cell line-based Transwell®-like models display an organ-specific epithelial barrier integrity, ultrastructural features and representative transport functions. Altogether, our novel model systems are cost-efficient with close similarity to the in vivo situation, therefore favoring their use in bioavailability studies in the context of pre-clinical screenings. 15 Online First
Keywords	cell line ; immortalization ; organoids ; Small intestinal tissue ; Transwell® models ; DDC::600 Technik ; Medizin ; angewandte Wissenschaften::610 Medizin und Gesundheit
Subject code	610
Language	English
Publishing country	de
Document type	Article ; Online
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Article ; Online: Hem1 is essential for ruffled border formation in osteoclasts and efficient bone resorption.

Werbenko, Eugenie / de Gorter, David J J / Kleimann, Simon / Beckmann, Denise / Waltereit-Kracke, Vanessa / Reinhardt, Julia / Geers, Fabienne / Paruzel, Peter / Hansen, Uwe / Pap, Thomas / Stradal, Theresia E B / Dankbar, Berno

Scientific reports

2024 Volume 14, Issue 1, Page(s) 8109

Abstract: Bone resorption is highly dependent on the dynamic rearrangement of the osteoclast actin cytoskeleton to allow formation of actin rings and a functional ruffled border. Hem1 is a hematopoietic-specific subunit of the WAVE-complex which regulates actin ... ...

Abstract	Bone resorption is highly dependent on the dynamic rearrangement of the osteoclast actin cytoskeleton to allow formation of actin rings and a functional ruffled border. Hem1 is a hematopoietic-specific subunit of the WAVE-complex which regulates actin polymerization and is crucial for lamellipodia formation in hematopoietic cell types. However, its role in osteoclast differentiation and function is still unknown. Here, we show that although the absence of Hem1 promotes osteoclastogenesis, the ability of Hem1
MeSH term(s)	Humans ; Osteoclasts/metabolism ; Actins/metabolism ; Bone Resorption/metabolism ; Bone and Bones/metabolism ; Osteogenesis
Chemical Substances	Actins
Language	English
Publishing date	2024-04-06
Publishing country	England
Document type	Journal Article
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-024-58110-x
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Article: Featuring... Theresia Stradal. Interview by Tine Walma.

Stradal, Theresia

FEBS letters

2006 Volume 580, Issue 12, Page(s) 2810

MeSH term(s)	Austria ; Cell Movement ; Germany ; Publishing
Language	English
Publishing date	2006-05-22
Publishing country	England
Document type	Comment ; Interview
ZDB-ID	212746-5
ISSN	1873-3468 ; 0014-5793
ISSN (online)	1873-3468
ISSN	0014-5793
DOI	10.1016/j.febslet.2006.04.075
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Article ; Online: Neurite Outgrowth-Inducing Drimane-Type Sesquiterpenoids Isolated from Cultures of the Polypore

Sum, Winnie Chemutai / Ebada, Sherif S / Kirchenwitz, Marco / Wanga, Lucy / Decock, Cony / Stradal, Theresia E B / Matasyoh, Josphat Clement / Mándi, Attila / Kurtán, Tibor / Stadler, Marc

Journal of natural products

2023 Volume 86, Issue 11, Page(s) 2457–2467

Abstract: Abundisporin A ( ...

Abstract	Abundisporin A (
MeSH term(s)	Molecular Structure ; Sesquiterpenes/chemistry ; Polyporaceae/chemistry ; Neuronal Outgrowth
Chemical Substances	drimane ; Sesquiterpenes
Language	English
Publishing date	2023-11-01
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	304325-3
ISSN	1520-6025 ; 0163-3864
ISSN (online)	1520-6025
ISSN	0163-3864
DOI	10.1021/acs.jnatprod.3c00525
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Article ; Online: Unreported cytochalasins from an acid-mediated transformation of cytochalasin J isolated from Diaporthe cf. ueckeri.

Kemkuignou, Blondelle Matio / Lambert, Christopher / Schmidt, Katharina / Schweizer, Lena / Anoumedem, Elodie Gisèle M / Kouam, Simeon F / Stadler, Marc / Stradal, Theresia / Marin-Felix, Yasmina

Fitoterapia

2023 Volume 166, Page(s) 105434

Abstract: Chemical investigation of an endophytic fungus herein identified as Diaporthe cf. ueckeri yielded four known compounds, named cytochalasins H and J and dicerandrols A and B. Reports of acid sensitivity within the cytochalasan family inspired an attempt ... ...

Abstract	Chemical investigation of an endophytic fungus herein identified as Diaporthe cf. ueckeri yielded four known compounds, named cytochalasins H and J and dicerandrols A and B. Reports of acid sensitivity within the cytochalasan family inspired an attempt of acid-mediated conversion of cytochalasins H and J, resulting in the acquisition of five polycyclic cytochalasins featuring 5/6/5/8-fused tetracyclic and 5/6/6/7/5-fused pentacyclic skeletons. Two of the obtained polycyclic cytochalasins constituted unprecedented analogues, for which the trivial names cytochalasins J
MeSH term(s)	Humans ; Molecular Structure ; Cytochalasins ; Antineoplastic Agents ; Fungi
Chemical Substances	cytochalasin J ; Cytochalasins ; Antineoplastic Agents
Language	English
Publishing date	2023-01-19
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	412385-2
ISSN	1873-6971 ; 0367-326X
ISSN (online)	1873-6971
ISSN	0367-326X
DOI	10.1016/j.fitote.2023.105434
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Article ; Online: Regulation of MRTF-A by JMY via a nucleation-independent mechanism.

Kluge, Franziska / Weissbach, Julia / Weber, Anja / Stradal, Theresia / Posern, Guido

Cell communication and signaling : CCS

2018 Volume 16, Issue 1, Page(s) 86

Abstract: Background: MRTF-A (myocardin-related transcription factor A) is a coactivator for SRF-mediated gene expression. The activity of MRTF-A is critically dependent on the dissociation of G-actin from N-terminal RPEL motifs. MRTF-SRF induction often ... ...

Abstract	Background: MRTF-A (myocardin-related transcription factor A) is a coactivator for SRF-mediated gene expression. The activity of MRTF-A is critically dependent on the dissociation of G-actin from N-terminal RPEL motifs. MRTF-SRF induction often correlates with enhanced polymerization of F-actin. Here we investigate MRTF regulation by the multifunctional JMY protein, which contains three WASP/verprolin homology 2 (WH2/V) domains and facilitates Arp2/3-dependent and -independent actin nucleation. Methods: Co-immunoprecipitation experiments, immunofluorescence and luciferase reporter assays were combined with selective inhibitors to investigate the effect of JMY and its domains on MRTF-A in NIH 3 T3 mouse fibroblasts. Results: JMY induced MRTF-A transcriptional activity and enhanced its nuclear translocation. Unexpectedly, MRTF-A was hyperactivated when the Arp2/3-recruiting CA region of JMY was deleted or mutated, suggesting an autoinhibitory mechanism for full-length JMY. Moreover, isolated WH2/V domains which are unable to nucleate actin were sufficient for nuclear accumulation and SRF activation. Recombinant WH2/V regions of JMY biochemically competed with MRTF-A for actin binding. Activation of MRTF-A by JMY was unaffected by Arp3 knockdown, by an Arp2/3 inhibitor, and by latrunculin which disassembles cellular F-actin. Restriction of JMY to the nucleus abrogated its MRTF-A activation. Finally, JMY RNAi reduced basal and stimulated transcriptional activation via MRTF-A. Conclusions: Our results suggest that JMY activates MRTF-SRF independently of F-actin via WH2/V-mediated competition with the RPEL region for G-actin binding in the cytoplasm. Furthermore, the C-terminal region facilitates an autoinhibitory effect on full-length JMY, possibly by intramolecular folding.
MeSH term(s)	Actins/metabolism ; Animals ; Cell Cycle Proteins ; Cytoplasm/metabolism ; Mice ; NIH 3T3 Cells ; Nuclear Proteins/metabolism ; Trans-Activators/metabolism
Chemical Substances	Actins ; Cell Cycle Proteins ; Jmy protein, mouse ; Mrtfa protein, mouse ; Nuclear Proteins ; Trans-Activators
Language	English
Publishing date	2018-11-21
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1478-811X
ISSN (online)	1478-811X
DOI	10.1186/s12964-018-0299-x
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