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Clusters of glycolipid and glycosylphosphatidylinositol‐anchored proteins in lymphoid cells : accumulation of actin regulated by local tyrosine phosphorylation

Clusters of glycolipid and glycosylphosphatidylinositol‐anchored proteins in lymphoid cells :... Lateral cross‐linking of glycosylphosphatidylinositol (GPI)‐anchored proteins and glycosphingolipids can trigger a signaling cascade which leads to activation of lymphoid cells. A possible explanation how the signal is transduced through the plasma membrane has arisen from the concept of raft sphingolipid‐cholesterol microdomains in cell membranes. Cross‐linking of GPI‐anchored proteins, glycolipids and other raft components leads to the formation of stabilized membrane patches in the plasma membrane which enrich members of the Src‐tyrosine kinase family. We have studied cellular responses to raft patch formation in the Jurkat T cell line and in particular changes in the actin cytoskeleton. We found that raft patches formed by GPI‐anchored CD59 protein and the ganglioside GM1 accumulate filamentous actin. Most interestingly, we observed a strong accumulation of tyrosine‐phosphorylated proteins in raft patches, strongly supporting the view that they can function as centers of signal transduction. Using a Lck kinase‐deficient variant of Jurkat cells and a specific Lck and Fyn tyrosine kinase inhibitor we found that enrichment of actin in raft patches is dependent on phosphotyrosine accumulation in the patches. These observations show a link between raft‐mediated signaling and the interaction of actin cytoskeleton with raft membrane domains. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png European Journal of Immunology Wiley

Clusters of glycolipid and glycosylphosphatidylinositol‐anchored proteins in lymphoid cells : accumulation of actin regulated by local tyrosine phosphorylation

Harder, Thomas; Simons, Kai
European Journal of Immunology , Volume 29 (2) – Feb 1, 1999
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References (28)

Publisher
Wiley
Copyright
© 1999 WILEY‐VCH Verlag GmbH, Weinheim, Fed. Rep. of Germany
ISSN
0014-2980
eISSN
1521-4141
DOI
10.1002/(SICI)1521-4141(199902)29:02<556::AID-IMMU556>3.0.CO;2-2
pmid
10064071
Publisher site
See Article on Publisher Site

Abstract

Lateral cross‐linking of glycosylphosphatidylinositol (GPI)‐anchored proteins and glycosphingolipids can trigger a signaling cascade which leads to activation of lymphoid cells. A possible explanation how the signal is transduced through the plasma membrane has arisen from the concept of raft sphingolipid‐cholesterol microdomains in cell membranes. Cross‐linking of GPI‐anchored proteins, glycolipids and other raft components leads to the formation of stabilized membrane patches in the plasma membrane which enrich members of the Src‐tyrosine kinase family. We have studied cellular responses to raft patch formation in the Jurkat T cell line and in particular changes in the actin cytoskeleton. We found that raft patches formed by GPI‐anchored CD59 protein and the ganglioside GM1 accumulate filamentous actin. Most interestingly, we observed a strong accumulation of tyrosine‐phosphorylated proteins in raft patches, strongly supporting the view that they can function as centers of signal transduction. Using a Lck kinase‐deficient variant of Jurkat cells and a specific Lck and Fyn tyrosine kinase inhibitor we found that enrichment of actin in raft patches is dependent on phosphotyrosine accumulation in the patches. These observations show a link between raft‐mediated signaling and the interaction of actin cytoskeleton with raft membrane domains.

Journal

European Journal of Immunology – Wiley

Published: Feb 1, 1999

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