The T cell antigen receptor activates phosphatidylinositol 3-kinase-regulated serine kinases protein kinase B and ribosomal S6 kinase 1

Autor: Virginie Lafont, Arian Laurence, Emmanuelle Astoul, Janny Liautard, Doreen A. Cantrell
Rok vydání: 2000
Předmět:
Glycogen synthase kinase-3
Morpholines
T-Lymphocytes
Receptors
Antigen
T-Cell
Biophysics
P70-S6 Kinase 1
Protein Serine-Threonine Kinases
Mitogen-activated protein kinase kinase
Biochemistry
Antibodies
MAP2K7
Glycogen Synthase Kinase 3
Phosphatidylinositol 3-Kinases
Phosphoserine
Protein kinase B
Structural Biology
Proto-Oncogene Proteins
Genetics
Humans
ASK1
c-Raf
Phosphorylation
Molecular Biology
Cells
Cultured
Phosphoinositide-3 Kinase Inhibitors
Sirolimus
MAP kinase kinase kinase
biology
Chemistry
Ribosomal Protein S6 Kinases
Cyclin-dependent kinase 2
Glycogen Synthase Kinases
Cell Biology
Molecular biology
Enzyme Activation
Molecular Weight
Chromones
Calcium-Calmodulin-Dependent Protein Kinases
biology.protein
Cyclin-dependent kinase 9
T cell receptor
Proto-Oncogene Proteins c-akt
Phosphatidylinositol 3-kinase
Ribosomal S6 kinase 1
Signal Transduction
Zdroj: FEBS Letters. 486:38-42
ISSN: 0014-5793
Popis: The present study has explored T cell antigen receptor-regulated serine kinases in human T cells. The results identify two phosphatidylinositol 3-kinase (PI3K)-controlled serine kinases operating downstream of the T cell receptor (TCR) in primary T cells: (i) protein kinase B whose activation regulates the phosphorylation of glycogen synthase kinase 3 and (ii) ribosomal S6 kinase 1, a kinase with a critical role in the regulation of protein synthesis and cell growth. T cells express two isoforms of S6k1: a 70 kDa cytoplasmic kinase and an 85 kDa isoform that has a classic nuclear localisation. TCR ligation triggers a parallel engagement of both the 70 and 85 kDa isoforms of S6k1 in a response that requires PI3K function.
Databáze: OpenAIRE
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