Tissue Transglutaminase Is an Integrin-Binding Adhesion Coreceptor for Fibronectin

@article{Akimov2000TissueTI,
  title={Tissue Transglutaminase Is an Integrin-Binding Adhesion Coreceptor for Fibronectin},
  author={Sergey Akimov and Dmitry Krylov and Laurie F. Fleischman and Alexey M. Belkin},
  journal={The Journal of Cell Biology},
  year={2000},
  volume={148},
  pages={825 - 838}
}
The protein cross-linking enzyme tissue transglutaminase binds in vitro with high affinity to fibronectin via its 42-kD gelatin-binding domain. Here we report that cell surface transglutaminase mediates adhesion and spreading of cells on the 42-kD fibronectin fragment, which lacks integrin-binding motifs. Overexpression of tissue transglutaminase increases its amount on the cell surface, enhances adhesion and spreading on fibronectin and its 42-kD fragment, enlarges focal adhesions, and… 
Cell-surface transglutaminase promotes fibronectin assembly via interaction with the gelatin-binding domain of fibronectin: a role in TGFbeta-dependent matrix deposition.
TLDR
The results implicate an interaction between transglutaminase and the gelatin-binding domain of fibronectin in matrix assembly and suggest its role in initiation of fibrillogenesis.
Cell-surface transglutaminase undergoes internalization and lysosomal degradation: an essential role for LRP1
TLDR
A previously unknown pathway of transglutaminase internalization and degradation that might be crucial for regulation of its adhesive and signaling functions on the cell surface is characterized and a novel functional link between cell-matrix adhesion and endocytosis is revealed.
Fibronectin-Tissue Transglutaminase Matrix Rescues RGD-impaired Cell Adhesion through Syndecan-4 and β1 Integrin Co-signaling*
TLDR
A model for a novel RGD-independent cell adhesion process that could be important during tissue injury and/or remodeling is proposed whereby TG-FN binding to syndecan-4 activates PKCα leading to its association with β1 integrin, reinforcement of actin-stress fiber organization, and MAPK pathway activation.
Cell surface transglutaminase promotes RhoA activation via integrin clustering and suppression of the Src-p190RhoGAP signaling pathway.
TLDR
Results show that surface tTG amplifies integrin-mediated signaling to RhoA/ROCK via integrin clustering and down-regulation of the Src-p190RhoGAP regulatory pathway.
A Novel RGD-independent Cell Adhesion Pathway Mediated by Fibronectin-bound Tissue Transglutaminase Rescues Cells from Anoikis*
TLDR
A novel RGD-independent cell adhesion mechanism that promotes cell survival when the anti-apoptotic role mediated byRGD-dependent integrin function is reduced as in tissue injury, which is consistent with the externalization and binding of tTG to fibronectin following cell damage/stress.
Cell surface tissue transglutaminase is involved in adhesion and migration of monocytic cells on fibronectin.
TLDR
Data demonstrate that cell surface tTG serves as an integrin-associated adhesion receptor that might be involved in extravasation and migration of monocytic cells into tissues containing Fn matrices during inflammation.
Transglutaminase-mediated oligomerization of the fibrin(ogen) alphaC domains promotes integrin-dependent cell adhesion and signaling.
TLDR
These findings provide new insights into the mechanism of the alphaC domain-mediated interaction of endothelial cells with fibrin and imply its potential involvement in cell migration and suggest a new role for transglutaminases in regulation of integrin-mediated adhesion and signaling via covalent modification ofIntegrin ligands.
Enhanced osteoblast adhesion on transglutaminase 2-crosslinked fibronectin
TLDR
It is hypothesized that TG2-mediated crosslinking enhances the cell-adhesive properties of FN by increasing the molecular rigidity of FN in the extracellular matrix.
Heparan Sulfate Proteoglycans Are Receptors for the Cell-surface Trafficking and Biological Activity of Transglutaminase-2
TLDR
It is proposed that the membrane trafficking of TG2, and hence its extracellular activity, is linked to TG2 binding to cell-surface HSPG.
Targeting Ovarian Tumor Cell Adhesion Mediated by Tissue Transglutaminase
Tissue transglutaminase (TG2) is a transpeptidase involved in protein cross-linking through generation of ϵ-(γ-glutamyl)lysine isopeptide bonds. It also promotes cell adhesion through interaction
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 54 REFERENCES
Transglutaminase-mediated processing of fibronectin by endothelial cell monolayers.
We studied the interaction of [125I]fibronectin with human umbilical vein endothelial cells. Endothelial cell monolayers cross-linked [125I]fibronectin which had been preadsorbed to gelatin-coated
Activation of Distinct α5β1-mediated Signaling Pathways by Fibronectin's Cell Adhesion and Matrix Assembly Domains
TLDR
The data demonstrate that the amino-terminal type I repeats of fibronectin bind to the α5β1 integrin and support cell adhesion, and suggest a new paradigm for integrin-mediated signaling, where distinct regions within one ligand can modulate outside-in signaling through the same integrin.
The Fibronectin-binding Domain of Transglutaminase (*)
TLDR
The fibronectin-combining site of the liver transglutaminase was investigated by testing fragments obtained from the parent protein by controlled digestion with endoproteinase Lys-C and residues 1-7 in the liver enzyme seem to be of particular importance for influencing its ability to bind to fibronECTin.
Affinity of human erythrocyte transglutaminase for a 42-kDa gelatin-binding fragment of human plasma fibronectin.
TLDR
Binding was remarkably specific and could be exploited for the affinity purification of transglutaminase directly from the hemoglobin-depleted erythrocyte lysate and might have general applicability in other systems involving separation of tightly bound ligands.
Reduced expression of tissue transglutaminase in a human endothelial cell line leads to changes in cell spreading, cell adhesion and reduced polymerisation of fibronectin.
TLDR
The results of these experiments suggest that externalised tTgase may play a key role in a number of cell behavioural patterns which might be related to the enzymes ability to bind and crosslink fibronectin.
Fibronectin Type III Repeats Mediate RGD-independent Adhesion and Signaling through Activated β1 Integrins*
TLDR
It is found that, after experimental activation of β1 integrins, a number of cell types adhere and spread on FNIII repeats lacking RGD, derived from extracellular matrix proteins and cytokine receptors.
Complexation of fibronectin with tissue transglutaminase.
TLDR
A stoichiometry of 2:1 is indicated for the binding of the human erythrocyte transglutaminase to human plasma fibronectin, suggesting that a domain on the transglUTaminase molecule other than the catalytic site is needed for complexation with fibronECTin.
Muscle β1D Integrin Reinforces the Cytoskeleton–Matrix Link: Modulation of Integrin Adhesive Function by Alternative Splicing
TLDR
Phenotypic effects of β1D integrin expression in nonmuscle cells are due to its enhanced interactions with both cytoskeletal and extracellular ligands, parallel the transitions that muscle cells undergo during differentiation.
Regulated expression of tissue transglutaminase in Swiss 3T3 fibroblasts: effects on the processing of fibronectin, cell attachment, and cell death.
TLDR
Modulation of expression of tTgase has indicated a possible physiological function for the enzyme in cell attachment, the crosslinking of fibronectin during fibril assembly, and the maintenance of cellular integrity in a novel form of cell death.
...
1
2
3
4
5
...