A Lipid Raft Environment Enhances Lyn Kinase Activity by Protecting the Active Site Tyrosine from Dephosphorylation
Open Access
- 1 June 2003
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 278 (23) , 20746-20752
- https://doi.org/10.1074/jbc.m211402200
Abstract
No abstract availableKeywords
This publication has 45 references indexed in Scilit:
- Fyn kinase initiates complementary signals required for IgE-dependent mast cell degranulationNature Immunology, 2002
- FcϵRI as a paradigm for a lipid raft-dependent receptor in hematopoietic cellsSeminars in Immunology, 2001
- Interaction between the Unphosphorylated Receptor with High Affinity for IgE and Lyn KinasePublished by Elsevier ,2001
- THE HIGH-AFFINITY IgE RECEPTOR (FcεRI): From Physiology to PathologyAnnual Review of Immunology, 1999
- Allergy-Associated FcRβ Is a Molecular Amplifier of IgE- and IgG-Mediated In Vivo ResponsesImmunity, 1998
- The Unique Domain as the Site on Lyn Kinase for Its Constitutive Association with the High Affinity Receptor for IgEPublished by Elsevier ,1997
- Compartmentalized Activation of the High Affinity Immunoglobulin E Receptor within Membrane DomainsJournal of Biological Chemistry, 1997
- The FcεRIβ Subunit Functions as an Amplifier of FcεRIγ-Mediated Cell Activation SignalsCell, 1996
- Aggregation of the high-affinity IgE receptor and enhanced activity of p53/56lyn protein-tyrosine kinase.Proceedings of the National Academy of Sciences, 1994
- Transphosphorylation as the mechanism by which the high-affinity receptor for IgE is phosphorylated upon aggregation.Proceedings of the National Academy of Sciences, 1994