Differential regulation of Src-family protein tyrosine kinases in GPI domains of T lymphocyte plasma membranes
| Autor: | Daniel C. Hoessli, Elisabeth Rungger-Brändle, Gerhild van Echten-Deckert, Subburaj Ilangumaran, Monique Poincelet, Stephan Arni, Anne Briol, Konrad Sandhoff |
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| Jazyk: | angličtina |
| Rok vydání: | 1996 |
| Předmět: |
src-Family Kinases/ metabolism
Glycosylphosphatidylinositols T-Lymphocytes Biophysics Biology ddc:616.07 Cell Fractionation Biochemistry Membrane Lipids Mice FYN Membrane Lipids/analysis/metabolism Animals Molecular Biology chemistry.chemical_classification Mice Inbred BALB C Kinase T-Lymphocytes/ metabolism Vesicle Cell Membrane Cell Biology Cell Membrane/chemistry/metabolism carbohydrates (lipids) Glycosylphosphatidylinositols/analysis/ metabolism src-Family Kinases Membrane chemistry Phosphorylation lipids (amino acids peptides and proteins) Cell fractionation Glycoprotein Proto-oncogene tyrosine-protein kinase Src Signal Transduction |
| Zdroj: | Biochemical and Biophysical Research Communications, Vol. 225, No 3 (1996) pp. 801-807 |
| ISSN: | 0006-291X |
| Popis: | The association of glycosylphosphatidylinositol (GPI)-anchored cell surface glycoproteins with Src-family protein tyrosine kinases was analysed in intact T lymphocyte plasma membranes. Following subcellular fractionation without detergent, 25% of the recovered plasma membranes were light density vesicles enriched in GPI-anchored glycoproteins and sphingolipids (GPI domains), while the remainder behaved as heavier density vesicles containing equal amounts of lipids and proteins. Qualitatively similar lipids were found in both vesicle types, but only light density vesicles made of 65-75% lipids yielded a Triton X-100 resistant, sedimentable fraction containing GPI-linked glycoproteins and sphingolipids. The GPI-rich vesicles phosphotyrosylated an exogenous substrate as efficiently as the denser vesicles, despite a low Lck and Fyn kinase content. Likewise, these kinases were more efficiently phosphorylated in GPI domains than in denser vesicles. GPI domains thus could constitute plasma membrane "hot spots" where associated Src kinases assume an optimally active conformation that contributes to signaling via GPI-anchored cell surface glycoproteins. |
| Databáze: | OpenAIRE |
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