Thy-1 glycoprotein and src-like protein-tyrosine kinase p53/p56lyn are associated in large detergent-resistant complexes in rat basophilic leukemia cells.

DOI Web Site 被引用文献8件
  • L Dráberová
    Department of Mammalian Gene Expression, Czechoslovak Academy of Sciences, Prague.
  • P Dráber
    Department of Mammalian Gene Expression, Czechoslovak Academy of Sciences, Prague.

書誌事項

公開日
1993-04-15
DOI
  • 10.1073/pnas.90.8.3611
公開者
Proceedings of the National Academy of Sciences

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<jats:p>Thy-1 is a surface glycoprotein that is attached to the plasma membrane by a glycosyl-phosphatidyl-inositol anchor. Crosslinking of Thy-1 in rat mast cells and basophilic leukemia cells (RBL-2H3) induces cell activation including histamine release and tyrosine phosphorylation of several proteins. Here we show that glycosyl-phosphatidylinositol-linked Thy-1 forms noncovalent complexes with src-related protein-tyrosine kinase p53/p56lyn and other protein-tyrosine kinases and/or their substrates. These complexes are resistant to solubilization by a nonionic detergent, sedimentable at 200,000 x g, and very large ( > 10 MDa) as determined by gel chromatography. Activation of RBL-2H3 cells by crosslinking of the high-affinity IgE receptors resulted in decreased recovery of the complexes. The combined data indicate the existence of large detergent-resistant domains in the surface membrane of mast cells that may play an important role in their activation.</jats:p>

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