scholarly journals Signal-Transducing Adaptor Protein-2 Regulates Integrin-Mediated T Cell Adhesion through Protein Degradation of Focal Adhesion Kinase

2007 ◽  
Vol 179 (4) ◽  
pp. 2397-2407 ◽  
Author(s):  
Yuichi Sekine ◽  
Satoshi Tsuji ◽  
Osamu Ikeda ◽  
Kenji Sugiyma ◽  
Kenji Oritani ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
T Cell ◽  
Protein Degradation ◽  
Focal Adhesion Kinase ◽  
Focal Adhesion ◽  
Adaptor Protein ◽  
T Cell Adhesion

scholarly journals The tyrosine phosphatase SHP-1 promotes T cell adhesion by activating the adaptor protein CrkII in the immunological synapse

2017 ◽  
Vol 10 (491) ◽  
pp. eaal2880 ◽  
Author(s):  
Inbar Azoulay-Alfaguter ◽  
Marianne Strazza ◽  
Michael Peled ◽  
Hila K. Novak ◽  
James Muller ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
T Cell ◽  
Immunological Synapse ◽  
Tyrosine Phosphatase ◽  
Adaptor Protein ◽  
T Cell Adhesion

scholarly journals The N terminus of SKAP55 enables T cell adhesion to TCR and integrin ligands via distinct mechanisms

2013 ◽  
Vol 203 (6) ◽  
pp. 1021-1041 ◽  
Author(s):  
Michael J. Ophir ◽  
Beiyun C. Liu ◽  
Stephen C. Bunnell
Keyword(s):  
Cell Adhesion ◽  
T Cell ◽  
T Cell Activation ◽  
Cell Activation ◽  
Adaptor Protein ◽  
Cell Receptor ◽  
Β1 Integrins ◽  
Src Homology ◽  
Integrin Ligands ◽  
T Cell Adhesion

The T cell receptor (TCR) triggers the assembly of “SLP-76 microclusters,” which mediate signals required for T cell activation. In addition to regulating integrin activation, we show that Src kinase–associated phosphoprotein of 55 kD (SKAP55) is required for microcluster persistence and movement, junctional stabilization, and integrin-independent adhesion via the TCR. These functions require the dimerization of SKAP55 and its interaction with the adaptor adhesion and degranulation-promoting adaptor protein (ADAP). A “tandem dimer” containing two ADAP-binding SKAP55 Src homology 3 (SH3) domains stabilized SLP-76 microclusters and promoted T cell adhesion via the TCR, but could not support adhesion to integrin ligands. Finally, the SKAP55 dimerization motif (DM) enabled the coimmunoprecipitation of the Rap1-dependent integrin regulator Rap1-GTP–interacting adaptor molecule (RIAM), the recruitment of talin into TCR-induced adhesive junctions, and “inside-out” signaling to β1 integrins. Our data indicate that SKAP55 dimers stabilize SLP-76 microclusters, couple SLP-76 to the force-generating systems responsible for microcluster movement, and enable adhesion via the TCR by mechanisms independent of RIAM, talin, and β1 integrins.

scholarly journals T cell adhesion and cytolysis of pancreatic cancer cells: a role for E-cadherin in immunotherapy?

2002 ◽  
Vol 87 (9) ◽  
pp. 1034-1041 ◽  
Author(s):  
J J French ◽  
J Cresswell ◽  
W K Wong ◽  
K Seymour ◽  
R M Charnley ◽  
...  
Keyword(s):  
Pancreatic Cancer ◽  
Cell Adhesion ◽  
T Cell ◽  
Cancer Cells ◽  
Pancreatic Cancer Cells ◽  
E Cadherin ◽  
T Cell Adhesion

scholarly journals The focal adhesion kinase inhibitor PF-562,271 impairs primary CD4+ T cell activation

2013 ◽  
Vol 86 (6) ◽  
pp. 770-781 ◽  
Author(s):  
Andrew J. Wiemer ◽  
Sarah A. Wernimont ◽  
Thai-duong Cung ◽  
David A. Bennin ◽  
Hilary E. Beggs ◽  
...  
Keyword(s):  
T Cell ◽  
Focal Adhesion Kinase ◽  
Focal Adhesion ◽  
T Cell Activation ◽  
Cell Activation ◽  
Kinase Inhibitor ◽  
Cd4 T Cell

Structural and ICAM-1-Docking Properties of a Cyclic Peptide from the I-domain of LFA-1: An inhibitor of ICAM-1/LFA-1-mediated T-cell adhesion

2002 ◽  
Vol 19 (5) ◽  
pp. 789-799 ◽  
Author(s):  
Christine R. Xu ◽  
Helena Yusuf-Makagiansar ◽  
Yongbo Hu ◽  
Seetharama D.S. Jois ◽  
Teruna J. Siahaan
Keyword(s):  
Cell Adhesion ◽  
T Cell ◽  
Cyclic Peptide ◽  
T Cell Adhesion

scholarly journals Augmentation of RANTES-Induced Extracellular Signal-Regulated Kinase Mediated Signaling and T Cell Adhesion by Elastase-Treated Fibronectin

2001 ◽  
Vol 166 (12) ◽  
pp. 7121-7127 ◽  
Author(s):  
Alexander Brill ◽  
Rami Hershkoviz ◽  
Gayle G. Vaday ◽  
Yehuda Chowers ◽  
Ofer Lider
Keyword(s):  
Cell Adhesion ◽  
T Cell ◽  
Extracellular Signal Regulated Kinase ◽  
Extracellular Signal ◽  
T Cell Adhesion

scholarly journals Candida albicans Expresses a Focal Adhesion Kinase-Like Protein That Undergoes Increased Tyrosine Phosphorylation upon Yeast Cell Adhesion to Vitronectin and the EA.hy 926 Human Endothelial Cell Line

2002 ◽  
Vol 70 (7) ◽  
pp. 3804-3815 ◽  
Author(s):  
Giorgio Santoni ◽  
Roberta Lucciarini ◽  
Consuelo Amantini ◽  
Jordan Jacobelli ◽  
Elisabetta Spreghini ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Candida Albicans ◽  
Cell Adhesion ◽  
Endothelial Cell ◽  
Yeast Cell ◽  
Focal Adhesion Kinase ◽  
Cell Line ◽  
Tyrosine Phosphorylation ◽  
Focal Adhesion ◽  
Human Endothelial Cell Line

ABSTRACT The signaling pathways triggered by adherence of Candida albicans to the host cells or extracellular matrix are poorly understood. We provide here evidence in C. albicans yeasts of a p105 focal adhesion kinase (Fak)-like protein (that we termed CaFak), antigenically related to the vertebrate p125Fak, and its involvement in integrin-like-mediated fungus adhesion to vitronectin (VN) and EA.hy 926 human endothelial cell line. Biochemical analysis with different anti-chicken Fak antibodies identified CaFak as a 105-kDa protein and immunofluorescence and cytofluorimetric analysis on permeabilized cells specifically stain C. albicans yeasts; moreover, confocal microscopy evidences CaFak as a cytosolic protein that colocalizes on the membrane with the integrin-like VN receptors upon yeast adhesion to VN. The protein tyrosine kinase (PTK) inhibitors genistein and herbimycin A strongly inhibited C. albicans yeast adhesion to VN and EA.hy 926 endothelial cells. Moreover, engagement of αvβ3 and αvβ5 integrin-like on C. albicans either by specific monoclonal antibodies or upon adhesion to VN or EA.hy 926 endothelial cells stimulates CaFak tyrosine phosphorylation that is blocked by PTK inhibitor. A role for CaFak in C. albicans yeast adhesion was also supported by the failure of VN to stimulate its tyrosine phosphorylation in a C. albicans mutant showing normal levels of CaFak and VNR-like integrins but displaying reduced adhesiveness to VN and EA.hy 926 endothelial cells. Our results suggest that C. albicans Fak-like protein is involved in the control of yeast cell adhesion to VN and endothelial cells.

scholarly journals Cell Adhesion and Focal Adhesion Kinase Regulate Insulin Receptor Substrate-1 Expression

2000 ◽  
Vol 275 (49) ◽  
pp. 38371-38377 ◽  
Author(s):  
Patricia Lebrun ◽  
Véronique Baron ◽  
Christof R. Hauck ◽  
David D. Schlaepfer ◽  
Emmanuel Van Obberghen
Keyword(s):  
Cell Adhesion ◽  
Insulin Receptor ◽  
Focal Adhesion Kinase ◽  
Focal Adhesion ◽  
Insulin Receptor Substrate ◽  
Insulin Receptor Substrate 1
Sign in / Sign up

Export Citation Format

Share Document