ArticleMolecular and cellular biochemistry2014
Type II phosphatidylinositol 4-kinases interact with FcεRIγ subunit in RBL-2H3 cells.
Article in Molecular and cellular biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed, 4 citations in OpenAlex.
- Type II PtdIns 4-kinase β associates with CD4-p56lck complex and is involved in CD4 receptor signaling.Molecular and cellular biochemistry · 2014Article
- Piperine inhibits type II phosphatidylinositol 4-kinases: a key component in phosphoinositides turnover.Molecular and cellular biochemistry · 2014Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
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.
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Registered trials
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