ArticleJournal of proteome research2011
Proteomics analysis of the ezrin interactome in B cells reveals a novel association with Myo18aα.
Article in Journal of proteome research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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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
8 citing papers in PubMed, 12 citations in OpenAlex.
- Role of Protein Kinase A Activation in the Immune System with an Emphasis on Lipopolysaccharide-Responsive and Beige-like Anchor Protein in B Cells.International journal of molecular sciences · 2023Review
- Cutting Edge: Myosin 18A Is a Novel Checkpoint Regulator in B Cell Differentiation and Antibody-Mediated Immunity.Journal of immunology (Baltimore, Md. : 1950) · 2021Article
- The ezrin-radixin-moesin family of proteins in the regulation of B-cell immune response.Critical reviews in immunology · 2015Review
- SP-R210 (Myo18A) Isoforms as Intrinsic Modulators of Macrophage Priming and Activation.PloS one · 2015Article
- Interactome analysis reveals ezrin can adopt multiple conformational states.The Journal of biological chemistry · 2013Article
- Functional characterization of human myosin-18A and its interaction with F-actin and GOLPH3.The Journal of biological chemistry · 2013Article
- Ezrin tunes the magnitude of humoral immunity.Journal of immunology (Baltimore, Md. : 1950) · 2013Article
- Proteomic analysis of α4β1 integrin adhesion complexes reveals α-subunit-dependent protein recruitment.Proteomics · 2012Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The molecular regulation of recruitment and assembly of signalosomes near the B cell receptor (BCR) is poorly understood. We have previously demonstrated a role for the ERM family protein ezrin in regulating antigen-dependent lipid raft coalescence in B cells. In this study, we addressed the possibility that ezrin may collaborate with other adaptor proteins to regulate signalosome dynamics at the membrane. Using mass spectrometry-based proteomics analysis, we identified Myo18aα as a novel binding partner of ezrin. Myo18aα is an attractive candidate as it has several protein-protein interaction domains and an intrinsic motor activity. The expression of Myo18aα varied during B cell development in the bone marrow and in mature B cell subsets suggesting functional differences. Interestingly, BCR stimulation increased the association between ezrin and Myo18aα, and induced co-segregation of Myo18aα with the BCR and phosphotyrosine-containing proteins. Our data raise an intriguing possibility that the Myo18aα/ezrin complex may facilitate BCR-mediated signaling by recruiting signaling proteins that are in close proximity of the antigen receptor. Our study is not only significant with respect to understanding the molecular regulation of BCR signaling but also provides a broader basis for understanding the mechanism of action of ezrin in other cellular systems.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.