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The general aim of our laboratory is to decipher signal transduction mechanisms that regulate T lymphocyte activation, function and differentiation into effector cells, as well as the characterisation of proto-oncogen products that are involved in cell transformation.
Immunophilins control T lymphocyte adhesion and migration by regulating C3G binding to CrkII. Crk adaptor proteins are key players in signal transduction from a variety of cell surface receptors. CrkI and CrkII, the two alternative-spliced forms of CRK, possess an N-terminal SH2 domain, followed by an SH3 domain, while CrkII possesses in addition a C-terminal linker region plus an SH3 domain, which operate as regulatory moieties. Here, we investigated the ability of immunophilins, that function as peptidyl-prolyl isomerases (PPIases), to regulate Crk proteins in human T lymphocytes. We found that endogenous CrkII, but not CrkI, associates with the immunophilins, cyclophilin A (CypA) and FKBP12, in resting human Jurkat T cells. In addition, CypA increased C3G binding to CrkII, while inhibitors of immunophilins, such as cyclosporine A (CsA) and FK506, inhibited CrkII, but not CrkI association with C3G. Expression in Jurkat T cells of PICCHUx, a plasmid encoding the human CrkII1-236 sandwiched between CFP and YFP, demonstrated a basal level of FRET, which increased in response to cell treatment with CsA and FK506, reflecting increased trans-to-cis conversion of CrkII. Crk-C3G complexes are known to play an important role in integrin-mediated cell adhesion and migration. We found that overexpression of CrkI or CrkII increased adhesion and migration of Jurkat T cells.
The general aim of our laboratory is to decipher signal transduction mechanisms that regulate T lymphocyte activation, function and differentiation into effector cells, as well as the characterisation of proto-oncogen products that are involved in cell transformation.
Immunophilins control T lymphocyte adhesion and migration by regulating C3G binding to CrkII. Crk adaptor proteins are key players in signal transduction from a variety of cell surface receptors. CrkI and CrkII, the two alternative-spliced forms of CRK, possess an N-terminal SH2 domain, followed by an SH3 domain, while CrkII possesses in addition a C-terminal linker region plus an SH3 domain, which operate as regulatory moieties. Here, we investigated the ability of immunophilins, that function as peptidyl-prolyl isomerases (PPIases), to regulate Crk proteins in human T lymphocytes. We found that endogenous CrkII, but not CrkI, associates with the immunophilins, cyclophilin A (CypA) and FKBP12, in resting human Jurkat T cells. In addition, CypA increased C3G binding to CrkII, while inhibitors of immunophilins, such as cyclosporine A (CsA) and FK506, inhibited CrkII, but not CrkI association with C3G. Expression in Jurkat T cells of PICCHUx, a plasmid encoding the human CrkII1-236 sandwiched between CFP and YFP, demonstrated a basal level of FRET, which increased in response to cell treatment with CsA and FK506, reflecting increased trans-to-cis conversion of CrkII. Crk-C3G complexes are known to play an important role in integrin-mediated cell adhesion and migration. We found that overexpression of CrkI or CrkII increased adhesion and migration of Jurkat T cells.
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Divya Ram Jayaram, Sigal Frost,Chanan Argov, Vijayasteltar Belsamma Liju,Nikhil Ponnoor Anto,Amitha Muraleedharan,Assaf Ben-Ari, Rose Sinay,Ilan Smoly,Ofra Novoplansky,Noah Isakov,Debra Toiber,
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Chenicheri Kizhakkeveettil Keerthana,Tennyson Prakash Rayginia, Sadiq Chembothumparambil Shifana,Nikhil Ponnoor Anto,Kalishwaralal Kalimuthu,Noah Isakov,Ruby John Anto
Exploration of immunology (2023)
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Frontiers in Oncology (2022): 812598
biorxiv(2022)
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