Type II phosphatidylinositol 4-kinases interact with FcεRIγ subunit in RBL-2H3 cells
| Autor: | Naveen Bojjireddy, Ranjeet Kumar Sinha, Gosukonda Subrahmanyam |
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| Rok vydání: | 2014 |
| Předmět: |
Protein subunit
Clinical Biochemistry Minor Histocompatibility Antigens chemistry.chemical_compound Membrane Microdomains Humans Amino Acid Sequence Mast Cells Phosphatidylinositol Phosphorylation Tyrosine Receptor Molecular Biology Lipid raft Receptors IgE Kinase Chemistry Cell Biology General Medicine Cell biology Phosphotransferases (Alcohol Group Acceptor) Biochemistry Mutation Signal transduction Cell activation Signal Transduction |
| Zdroj: | Molecular and Cellular Biochemistry. 390:197-203 |
| ISSN: | 1573-4919 0300-8177 |
| DOI: | 10.1007/s11010-014-1970-1 |
| Popis: | Ligation of high-affinity IgE receptor I (FcεRI) on RBL-2H3 cells leads to recruitment of FcεRI and type II phosphatidylinositol 4-kinases (PtdIns 4-kinases) into lipid rafts. Lipid raft integrity is required for the activation of type II PtdIns 4-kinases and signal transduction through FcεRIγ during RBL-2H3 cell activation. However, the molecular mechanism by which PtdIns 4-kinases are coupled to FcεRI signaling is elusive. Here, we report association of type II PtdIns 4-kinase activity with FcεRIγ subunit in anti-FcεRIγ immunoprecipitates. FcεRIγ-associated PtdIns 4-kinase activity increases threefold upon FcεRI ligation in anti-FcεRIγ immunoprecipitates. Biochemical characterization of PtdIns 4-kinase activity associated with FcεRIγ reveals that it is a type II PtdIns 4-kinases. Canonical tyrosine residues mutation in FcεRIγ ITAM (Y65 and Y76) reveals that these two tyrosine residues in γ subunit are required for its interaction with type II PtdIns 4-kinases. |
| Databáze: | OpenAIRE |
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