Loading…

GPI-Anchored Cell-Surface Molecules Complexed to Protein Tyrosine Kinases

Binding of ligand or antibody to certain cell-surface proteins that are anchored to the membrane by glycophosphatidylinositol (GPI) can cause activation of leukocytes. However, it is not known how these molecules, which lack intracellular domains, can transduce signals. The GPI-linked human molecule...

Full description

Saved in:
Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 1991-11, Vol.254 (5034), p.1016-1019
Main Authors: S̆tefanová, Irena, Hor̆ejs̆i, Václav, Ansotegui, Ignacio J., Knapp, Walter, Stockinger, Hannes
Format: Article
Language:English
Subjects:
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Binding of ligand or antibody to certain cell-surface proteins that are anchored to the membrane by glycophosphatidylinositol (GPI) can cause activation of leukocytes. However, it is not known how these molecules, which lack intracellular domains, can transduce signals. The GPI-linked human molecules CD59, CD55, CD48, CD24, and CD14 as well as the mouse molecules Thy-1 and Ly-6 were found to associate with protein tyrosine kinases, key regulators of cell activation and signal transduction. A protein tyrosine kinase associated with the GPI-linked proteins CD59, CD55, and CD48 in human T cells, and with Thy-1 in mouse T cells was identified as p56$^{lck}$, a protein tyrosine kinase related to Src. This interaction of GPI-linked molecules with protein tyrosine kinases suggests a potential mechanism of signal transduction in cells.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.1719635