LIVIVO - Search results -

Search results

Result 1 - 10 of total 355

Search options

Article ; Online: KANK proteins.

Guo, Shiny Shengzhen / Fässler, Reinhard

2022 Volume 32, Issue 19, Page(s) R990–R992

MeSH term(s)	Adaptor Proteins, Signal Transducing ; Cytoskeletal Proteins
Chemical Substances	Adaptor Proteins, Signal Transducing ; Cytoskeletal Proteins
Language	English
Publishing date	2022-10-11
Publishing country	England
Document type	Journal Article
ZDB-ID	1071731-6
ISSN	1879-0445 ; 0960-9822
ISSN (online)	1879-0445
ISSN	0960-9822
DOI	10.1016/j.cub.2022.08.073
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 3208: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
Jg. 1995 - 2021: Lesesall (2.OG)
ab Jg. 2022: Lesesaal (EG)

Order via subito

This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: β1 integrin-mediated mast cell immune-surveillance of blood vessel content.

Link, Kristina / Muhandes, Lina / Polikarpova, Anastasia / Lämmermann, Tim / Sixt, Michael / Fässler, Reinhard / Roers, Axel

The Journal of allergy and clinical immunology

2024

Abstract: Background: Immunoglobulin E, IgE)-mediated degranulation of mast cells, MCs) provides rapid protection against environmental hazards, including animal venoms. A fraction of tissue-resident MCs intimately associates with blood vessels. These ... ...

Abstract	Background: Immunoglobulin E, IgE)-mediated degranulation of mast cells, MCs) provides rapid protection against environmental hazards, including animal venoms. A fraction of tissue-resident MCs intimately associates with blood vessels. These perivascular MCs were reported to extend projections into the vessel lumen and to be the first MCs to acquire intravenously injected IgE, suggesting that IgE loading of MCs depends on their vascular association. Objective: We sought to elucidate the molecular basis of the MC-blood vessel interaction and to determine its relevance for IgE-mediated immune responses. Methods: We selectively inactivated the Itgb1 gene, encoding the β1 chain of integrin adhesion molecules, ITGB1; in MCs by conditional gene targeting in mice. We analyzed skin MCs for blood vessel association, surface IgE density, capability to bind circulating antibody specific for MC surface molecules, as well as in vivo responses to antigen administered via different routes. Results: Lack of ITGB1 expression severely compromised MC blood vessel association. ITGB1-deficient MCs showed normal densities of surface IgE but reduced binding of intravenously injected antibodies. While their capacity to degranulate in response to IgE ligation in vivo was unimpaired, anaphylactic responses to antigen circulating in the vasculature were largely abolished. Conclusion: ITGB1-mediated association of MCs with blood vessels is key for MC immune-surveillance of blood vessel content, but is dispensable for slow steady-state loading of endogenous IgE onto tissue-resident MCs.
Language	English
Publishing date	2024-04-15
Publishing country	United States
Document type	Journal Article
ZDB-ID	121011-7
ISSN	1097-6825 ; 1085-8725 ; 0091-6749
ISSN (online)	1097-6825 ; 1085-8725
ISSN	0091-6749
DOI	10.1016/j.jaci.2024.03.022
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Uh III Zs.92: Show issues

Location:
Je nach Verfügbarkeit (siehe Angabe bei Bestand)
bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular
ab Jg. 2022: Lesesaal (EG)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Talin and kindlin use integrin tail allostery and direct binding to activate integrins.

Aretz, Jonas / Aziz, Masood / Strohmeyer, Nico / Sattler, Michael / Fässler, Reinhard

Nature structural & molecular biology

2023 Volume 30, Issue 12, Page(s) 1913–1924

Abstract: Integrin affinity regulation, also termed integrin activation, is essential for metazoan life. Although talin and kindlin binding to the β-integrin cytoplasmic tail is indispensable for integrin activation, it is unknown how they achieve this function. ... ...

Abstract	Integrin affinity regulation, also termed integrin activation, is essential for metazoan life. Although talin and kindlin binding to the β-integrin cytoplasmic tail is indispensable for integrin activation, it is unknown how they achieve this function. By combining NMR, biochemistry and cell biology techniques, we found that talin and kindlin binding to the β-tail can induce a conformational change that increases talin affinity and decreases kindlin affinity toward it. We also discovered that this asymmetric affinity regulation is accompanied by a direct interaction between talin and kindlin, which promotes simultaneous binding of talin and kindlin to β-tails. Disrupting allosteric communication between the β-tail-binding sites of talin and kindlin or their direct interaction in cells severely compromised integrin functions. These data show how talin and kindlin cooperate to generate a small but critical population of ternary talin-β-integrin-kindlin complexes with high talin-integrin affinity and high dynamics.
MeSH term(s)	Animals ; Talin/chemistry ; Talin/metabolism ; Integrins/metabolism ; Binding Sites ; Protein Binding
Chemical Substances	Talin ; Integrins
Language	English
Publishing date	2023-12-12
Publishing country	United States
Document type	Journal Article
ZDB-ID	2126708-X
ISSN	1545-9985 ; 1545-9993
ISSN (online)	1545-9985
ISSN	1545-9993
DOI	10.1038/s41594-023-01139-9
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 4101: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 56: Show issues

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: CDK1-cyclin-B1-induced kindlin degradation drives focal adhesion disassembly at mitotic entry.

Chen, Nan-Peng / Aretz, Jonas / Fässler, Reinhard

Nature cell biology

2022 Volume 24, Issue 5, Page(s) 723–736

Abstract: The disassembly of integrin-containing focal adhesions (FAs) at mitotic entry is essential for cell rounding, mitotic retraction fibre formation, bipolar spindle positioning and chromosome segregation. The mechanism that drives FA disassembly at mitotic ... ...

Abstract	The disassembly of integrin-containing focal adhesions (FAs) at mitotic entry is essential for cell rounding, mitotic retraction fibre formation, bipolar spindle positioning and chromosome segregation. The mechanism that drives FA disassembly at mitotic entry is unknown. Here, we show that the CDK1-cyclin B1 complex phosphorylates the integrin activator kindlin, which results in the recruitment of the cullin 9-FBXL10 ubiquitin ligase complex that mediates kindlin ubiquitination and degradation. This molecular pathway is essential for FA disassembly and cell rounding, as phospho-inhibitory mutations of the CDK1 motif prevent kindlin degradation, FA disassembly and mitotic cell rounding. Conversely, phospho-mimetic mutations promote kindlin degradation in interphase, accelerate mitotic cell rounding and impair mitotic retraction fibre formation. Despite the opposing effects on kindlin stability, both types of mutations cause severe mitotic spindle defects, apoptosis and aneuploidy. Thus, the exquisite regulation of kindlin levels at mitotic entry is essential for cells to progress accurately through mitosis.
MeSH term(s)	CDC2 Protein Kinase/genetics ; CDC2 Protein Kinase/metabolism ; Cell Cycle Proteins/metabolism ; Cyclin B1/genetics ; Cyclin B1/metabolism ; Focal Adhesions/genetics ; Focal Adhesions/metabolism ; Integrins/metabolism ; Mitosis/genetics ; Phosphorylation ; Spindle Apparatus/genetics ; Spindle Apparatus/metabolism
Chemical Substances	Cell Cycle Proteins ; Cyclin B1 ; Integrins ; CDC2 Protein Kinase (EC 2.7.11.22)
Language	English
Publishing date	2022-04-25
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1474722-4
ISSN	1476-4679 ; 1465-7392
ISSN (online)	1476-4679
ISSN	1465-7392
DOI	10.1038/s41556-022-00886-z
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 5169: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
Zs.MG 12: Show issues

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Integrin β1 regulates marginal zone B cell differentiation and PI3K signaling.

Andreani, Virginia / Ramamoorthy, Senthilkumar / Fässler, Reinhard / Grosschedl, Rudolf

The Journal of experimental medicine

2022 Volume 220, Issue 1

Abstract: Marginal zone (MZ) B cells represent innate-like B cells that mediate a fast immune response. The adhesion of MZ B cells to the marginal sinus of the spleen is governed by integrins. Here, we address the question of whether β1-integrin has additional ... ...

Abstract	Marginal zone (MZ) B cells represent innate-like B cells that mediate a fast immune response. The adhesion of MZ B cells to the marginal sinus of the spleen is governed by integrins. Here, we address the question of whether β1-integrin has additional functions by analyzing Itgb1fl/flCD21Cre mice in which the β1-integrin gene is deleted in mature B cells. We find that integrin β1-deficient mice have a defect in the differentiation of MZ B cells and plasma cells. We show that integrin β1-deficient transitional B cells, representing the precursors of MZ B cells, have enhanced B cell receptor (BCR) signaling, altered PI3K and Ras/ERK pathways, and an enhanced interaction of integrin-linked kinase (ILK) with the adaptor protein Grb2. Moreover, the MZ B cell defect of integrin β1-deficient mice could, at least in part, be restored by a pharmacological inhibition of the PI3K pathway. Thus, β1-integrin has an unexpected function in the differentiation and function of MZ B cells.
MeSH term(s)	Mice ; Animals ; Integrin beta1/metabolism ; Phosphatidylinositol 3-Kinases/metabolism ; Signal Transduction ; Cell Differentiation ; Integrins
Chemical Substances	Integrin beta1 ; Phosphatidylinositol 3-Kinases (EC 2.7.1.-) ; Integrins
Language	English
Publishing date	2022-11-09
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	218343-2
ISSN	1540-9538 ; 0022-1007
ISSN (online)	1540-9538
ISSN	0022-1007
DOI	10.1084/jem.20220342
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Ua VI Zs.107: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 2021: Bestellungen von Artikeln über das Online-Bestellformular ab Jg. 2022: Lesesaal (EG)
Zs.MG 45: Show issues

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: A FAK conundrum is solved: activation and organization of focal adhesion kinase at the plasma membrane.

Brod, Florian / Fässler, Reinhard

The EMBO journal

2020 Volume 39, Issue 19, Page(s) e106234

Abstract: Focal adhesion kinase (FAK) is a central mediator of cell adhesion, acting both as a scaffold and as catalytically active kinase. Acebrón et al (2020) use cryo-electron microscopy (cryo-EM) to visualize the dramatic structural changes that occur upon FAK ...

Abstract	Focal adhesion kinase (FAK) is a central mediator of cell adhesion, acting both as a scaffold and as catalytically active kinase. Acebrón et al (2020) use cryo-electron microscopy (cryo-EM) to visualize the dramatic structural changes that occur upon FAK recruitment to the plasma membrane, which releases FAK autoinhibition and induces its oligomerization. Since activity control via autoinhibition and protein clustering are features also utilized by other focal adhesion (FA) proteins, they have moved center stage in the endeavor to understand the complex process of cell adhesion regulation.
MeSH term(s)	Cell Adhesion ; Cell Membrane ; Cryoelectron Microscopy ; Focal Adhesion Kinase 1 ; Focal Adhesion Protein-Tyrosine Kinases ; Lipids ; Phosphorylation ; Signal Transduction
Chemical Substances	Lipids ; Focal Adhesion Kinase 1 (EC 2.7.10.2) ; Focal Adhesion Protein-Tyrosine Kinases (EC 2.7.10.2)
Language	English
Publishing date	2020-08-31
Publishing country	England
Document type	News ; Comment
ZDB-ID	586044-1
ISSN	1460-2075 ; 0261-4189
ISSN (online)	1460-2075
ISSN	0261-4189
DOI	10.15252/embj.2020106234
Database	MEDical Literature Analysis and Retrieval System OnLINE

Full text online

Accessible to users with ZB MED library card

In stock of ZB MED Cologne/Königswinter

Zs.A 1808: 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)
Zs.MG 100: Show issues

Order via subito

Details ▾

Article ; Online: In mitosis integrins reduce adhesion to extracellular matrix and strengthen adhesion to adjacent cells.

Huber, Maximilian / Casares-Arias, Javier / Fässler, Reinhard / Müller, Daniel J / Strohmeyer, Nico

Nature communications

2023 Volume 14, Issue 1, Page(s) 2143

Abstract: To enter mitosis, most adherent animal cells reduce adhesion, which is followed by cell rounding. How mitotic cells regulate adhesion to neighboring cells and extracellular matrix (ECM) proteins is poorly understood. Here we report that, similar to ... ...

Abstract	To enter mitosis, most adherent animal cells reduce adhesion, which is followed by cell rounding. How mitotic cells regulate adhesion to neighboring cells and extracellular matrix (ECM) proteins is poorly understood. Here we report that, similar to interphase, mitotic cells can employ integrins to initiate adhesion to the ECM in a kindlin- and talin-dependent manner. However, unlike interphase cells, we find that mitotic cells cannot engage newly bound integrins to actomyosin via talin or vinculin to reinforce adhesion. We show that the missing actin connection of newly bound integrins leads to transient ECM-binding and prevents cell spreading during mitosis. Furthermore, β1 integrins strengthen the adhesion of mitotic cells to adjacent cells, which is supported by vinculin, kindlin, and talin1. We conclude that this dual role of integrins in mitosis weakens the cell-ECM adhesion and strengthens the cell-cell adhesion to prevent delamination of the rounding and dividing cell.
MeSH term(s)	Animals ; Integrins/metabolism ; Vinculin/metabolism ; Talin/metabolism ; Cell Adhesion/physiology ; Extracellular Matrix/metabolism ; Mitosis
Chemical Substances	Integrins ; Vinculin (125361-02-6) ; Talin
Language	English
Publishing date	2023-04-14
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/s41467-023-37760-x
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Article ; Online: Surface-induced phase separation of reconstituted nascent integrin clusters on lipid membranes.

Hsu, Chiao-Peng / Aretz, Jonas / Hordeichyk, Arsenii / Fässler, Reinhard / Bausch, Andreas R

Proceedings of the National Academy of Sciences of the United States of America

2023 Volume 120, Issue 31, Page(s) e2301881120

Abstract: Integrin adhesion complexes are essential membrane-associated cellular compartments for metazoan life. The formation of initial integrin adhesion complexes is a dynamic process involving focal adhesion proteins assembled at the integrin cytoplasmic tails ...

Abstract	Integrin adhesion complexes are essential membrane-associated cellular compartments for metazoan life. The formation of initial integrin adhesion complexes is a dynamic process involving focal adhesion proteins assembled at the integrin cytoplasmic tails and the inner leaflet of the plasma membrane. The weak multivalent protein interactions within the complex and with the plasma membrane suggest that liquid-liquid phase separation could play a role in the nascent adhesion assembly. Here, we report that solid-supported lipid membranes supplemented with phosphoinositides induce the phase separation of minimal integrin adhesion condensates composed of integrin
MeSH term(s)	Animals ; Integrins/metabolism ; Paxillin/metabolism ; Talin/metabolism ; Cell Membrane/metabolism ; Integrin beta1/metabolism ; Phosphatidylinositols ; Cell Adhesion/physiology
Chemical Substances	Integrins ; Paxillin ; Talin ; Integrin beta1 ; Phosphatidylinositols
Language	English
Publishing date	2023-07-26
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.2301881120
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 1148: 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)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: Kindlin stabilizes the talin·integrin bond under mechanical load by generating an ideal bond.

Bodescu, Mihai Adrian / Aretz, Jonas / Grison, Marco / Rief, Matthias / Fässler, Reinhard

Proceedings of the National Academy of Sciences of the United States of America

2023 Volume 120, Issue 26, Page(s) e2218116120

Abstract: Integrin-mediated adhesion is essential for metazoan life. Integrin binding to ligand requires an activation step prior to binding ligand that depends on direct binding of talin and kindlin to the β-integrin cytoplasmic tail and the transmission of force ...

Abstract	Integrin-mediated adhesion is essential for metazoan life. Integrin binding to ligand requires an activation step prior to binding ligand that depends on direct binding of talin and kindlin to the β-integrin cytoplasmic tail and the transmission of force from the actomyosin via talin to the integrin-ligand bonds. However, the affinity of talin for integrin tails is low. It is therefore still unclear how such low-affinity bonds are reinforced to transmit forces up to 10 to 40 pN. In this study, we use single-molecule force spectroscopy by optical tweezers to investigate the mechanical stability of the talin•integrin bond in the presence and absence of kindlin. While talin and integrin alone form a weak and highly dynamic slip bond, the addition of kindlin-2 induces a force-independent, ideal talin•integrin bond, which relies on the steric proximity of and the intervening amino acid sequences between the talin- and kindlin-binding sites in the β-integrin tail. Our findings show how kindlin cooperates with talin to enable transmission of high forces required to stabilize cell adhesion.
MeSH term(s)	Animals ; Talin/metabolism ; Integrins ; Ligands ; Membrane Proteins/metabolism ; Cell Adhesion
Chemical Substances	Talin ; Integrins ; Ligands ; Membrane Proteins
Language	English
Publishing date	2023-06-20
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.2218116120
Database	MEDical Literature Analysis and Retrieval System OnLINE

In stock of ZB MED Cologne/Königswinter

Zs.A 1148: 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)

Order via subito

Details ▾
- See ZB MED holdings
- Order with fees

Article ; Online: New insights into the phosphorylation of the threonine motif of the β1 integrin cytoplasmic domain.

Böttcher, Ralph T / Strohmeyer, Nico / Aretz, Jonas / Fässler, Reinhard

Life science alliance

2022 Volume 5, Issue 4

Abstract: Integrins require an activation step before ligand binding and signaling that is mediated by talin and kindlin binding to the β integrin cytosolic domain (β-tail). Conflicting reports exist about the contribution of phosphorylation of a conserved ... ...

Abstract	Integrins require an activation step before ligand binding and signaling that is mediated by talin and kindlin binding to the β integrin cytosolic domain (β-tail). Conflicting reports exist about the contribution of phosphorylation of a conserved threonine motif in the β1-tail (β1-pT788/pT789) to integrin activation. We show that widely used and commercially available antibodies against β1-pT788/pT789 integrin do not detect specific β1-pT788/pT789 integrin signals in immunoblots of several human and mouse cell lysates but bind bi-phosphorylated threonine residues in numerous proteins, which were identified by mass spectrometry experiments. Furthermore, we found that fibroblasts and epithelial cells expressing the phospho-mimicking β1-TT788/789DD integrin failed to activate β1 integrins and displayed reduced integrin ligand binding, adhesion initiation and cell spreading. These cellular defects are specifically caused by the inability of kindlin to bind β1-tail polypeptides carrying a phosphorylated threonine motif or phospho-mimicking TT788/789DD substitutions. Our findings indicate that the double-threonine motif in β1-class integrins is not a major phosphorylation site but if phosphorylated would curb integrin function.
MeSH term(s)	Amino Acid Motifs/physiology ; Animals ; Cells, Cultured ; Fibroblasts/metabolism ; Humans ; Integrin beta1/chemistry ; Integrin beta1/metabolism ; Mice ; Phosphorylation ; Threonine/chemistry ; Threonine/metabolism
Chemical Substances	Integrin beta1 ; Threonine (2ZD004190S)
Language	English
Publishing date	2022-01-07
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	2575-1077
ISSN (online)	2575-1077
DOI	10.26508/lsa.202101301
Database	MEDical Literature Analysis and Retrieval System OnLINE

Order via subito

Inter-library loan at ZB MED

Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

To top

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

Full text online

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

In stock of ZB MED Cologne/Königswinter

Order via subito

More links

Kategorien

Order via subito

Inter-library loan at ZB MED