Proteomics Analysis of the Ezrin Interactome in B Cells Reveals a Novel Association with Myo18aα
Interactome
DOI:
10.1021/pr200577d
Publication Date:
2011-07-14T01:44:23Z
AUTHORS (5)
ABSTRACT
The molecular regulation of recruitment and assembly signalosomes near the B cell receptor (BCR) is poorly understood. We have previously demonstrated a role for ERM family protein ezrin in regulating antigen-dependent lipid raft coalescence cells. In this study, we addressed possibility that may collaborate with other adaptor proteins to regulate signalosome dynamics at membrane. Using mass spectrometry-based proteomics analysis, identified Myo18aα as novel binding partner ezrin. an attractive candidate it has several protein-protein interaction domains intrinsic motor activity. expression varied during development bone marrow mature subsets suggesting functional differences. Interestingly, BCR stimulation increased association between Myo18aα, induced co-segregation phosphotyrosine-containing proteins. Our data raise intriguing Myo18aα/ezrin complex facilitate BCR-mediated signaling by recruiting are close proximity antigen receptor. study not only significant respect understanding but also provides broader basis mechanism action cellular systems.
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