Rap1 Is a Potent Activation Signal for Leukocyte Function-Associated Antigen 1 Distinct from Protein Kinase C and Phosphatidylinositol-3-OH Kinase

@article{Katagiri2000Rap1IA,
  title={Rap1 Is a Potent Activation Signal for Leukocyte Function-Associated Antigen 1 Distinct from Protein Kinase C and Phosphatidylinositol-3-OH Kinase},
  author={K. Katagiri and M. Hattori and N. Minato and S. Irie and K. Takatsu and T. Kinashi},
  journal={Molecular and Cellular Biology},
  year={2000},
  volume={20},
  pages={1956 - 1969}
}
ABSTRACT To identify the intracellular signals which increase the adhesiveness of leukocyte function-associated antigen 1 (LFA-1), we established an assay system for activation-dependent adhesion through LFA-1/intercellular adhesion molecule 1 ICAM-1 using mouse lymphoid cells reconstituted with human LFA-1 and then introduced constitutively active forms of signaling molecules. We found that the phorbol myristate acetate (PMA)-responsive protein kinase C (PKC) isotypes (α, βI, βII, and δ) or… Expand
Rap1-mediated Lymphocyte Function-associated Antigen-1 Activation by the T Cell Antigen Receptor Is Dependent on Phospholipase C-γ1*
TLDR
It is demonstrated that phospholipase C (PLC)-γ1 plays a critical role in the signaling pathway leading to Rap1 activation triggered by the TCR, and that TCR activation of Rap1 depends on CalDAG-GEFI, which is likely to activate LFA-1. Expand
Rap1 Functions as a Key Regulator of T-Cell and Antigen-Presenting Cell Interactions and Modulates T-Cell Responses
TLDR
It is shown that Rap1 is activated in T cells in an antigen-dependent manner and accumulated at the contact site of T-cell and antigen-loaded APC and that the activation state of Rap1 has a decisive effect on the T- cell response to antigen. Expand
PKC-theta selectively controls the adhesion-stimulating molecule Rap1.
TLDR
Data define that, among other pathways acting on LFA-1 regulation, PKC- theta and its effector RapGEF2 are critical factors in TCR signaling to Rap1. Expand
Phosphorylation of the LFA-1 Integrin β2-Chain on Thr-758 Leads to Adhesion, Rac-1/Cdc42 Activation, and Stimulation of CD69 Expression in Human T Cells*
TLDR
The results show that Thr-758-phosphorylated LFA-1 is upstream of Rac-1/Cdc42, cell adhesion, and costimulatory activation of human T cells, thus identifying phosphorylation of Thr-782 in β2 as a proximal element in L FA-1 signaling. Expand
The M-Ras-RA-GEF-2-Rap1 pathway mediates tumor necrosis factor-alpha dependent regulation of integrin activation in splenocytes.
TLDR
This work shows that RA-GEF-2 is specifically responsible for the activation of Rap1 that mediates tumor necrosis factor-alpha (TNF-alpha)-triggered integrin activation, and proves a crucial role of the cross-talk between two Ras-family GTPases M-Ras and Rap1, mediated by RA- GEf-2, in adhesion signaling. Expand
Regulation of Leukocyte Function-Associated Antigen 1-Mediated Adhesion by Somatostatin and Substance P in Mouse Spleen Cells
TLDR
It is suggested that SOM treatment of spleen cells, especially in CD8+ T cells, leads to downregulation of LFA-1 mRNA translation, inside-out signaling molecules for integrins (Ras, Rap1 and PI 3-kinase, but not PKC), and consequently to a decrease in the L FA-1-mediated adhesion to ICAM-1. Expand
The integrin linked kinase is required for chemokine-triggered high affinity conformation of neutrophil β2-integrin LFA1.
TLDR
Genetic deletion of the known kindlin-interactor integrin linked kinase (ILK) impaired neutrophil adhesion and extravasation in the cremaster muscle and in a clinically relevant model of renal-ischemia-reperfusion injury. Expand
The GTPase Rap1 Regulates Phorbol 12-Myristate 13-Acetate-stimulated but Not Ligand-induced β1Integrin-dependent Leukocyte Adhesion*
TLDR
This report identifies Rap1, not RhoA, as a critical geranylgeranylated protein mediating phorbol ester-stimulated β1 and β2integrin-dependent adhesion of Jurkat cells. Expand
The Small GTPase Rap1 Is Required for Mn2+- and Antibody-induced LFA-1- and VLA-4-mediated Cell Adhesion*
TLDR
It is suggested that Rap1 determines the functional availability of integrins for productive binding to integrin ligands and that available levels of GTP-bound Rap1 are required for the direct activation of LFA-1 and VLA-4. Expand
Rap1 Is Activated by Erythropoietin or Interleukin-3 and Is Involved in Regulation of β1 Integrin-mediated Hematopoietic Cell Adhesion*
TLDR
The results suggest that Epo and IL-3 activate Rap1 at least partly through the CrkL-C3G complex as well as through additional pathways most likely involving phospholipase Cγ and strongly implicate Rap1 in regulation of β1integrin-mediated hematopoietic cell adhesion. Expand
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