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Updated: May 26, 2026

Isolation of Labile Multi-protein Complexes by in vivo Controlled Cellular Cross-Linking and Immuno-magnetic Affinity Chromatography
Published on: March 10, 2010
[Identification of proteins interacting with adaptor protein Bam32]
1Department of Microbiology, Third Military Medical University, Chongqing 400038, China. xiaoxing@mail.tmmu.com.cn
Aim:
To study the role of adaptor protein Bam32 in B cell antigen receptor (BCR) signaling cascades.
Methods:
Using full length Bam32 as bait, yeast two-hybrid technique was used to screen the protein that could interact with Bam32. The interaction was further confirmed by co-transfection of 293T cells and coimmunoprecipitation.
Results:
Protein tyrosine kinase Lyn was one of the strong positive clones identified by the yeast two-hybrid screening. This interaction was further confirmed in 293T cells by co-transfection and coimmunoprecipitation. By using specific anti-phosphotyrosine antibody, it was found that Bam32 could be phosphorylated by Lyn.
Conclusion:
The interaction of Bam32 with Lyn leads to Bam32 phosphorylation, which might play an important role in activating downstream signaling molecules.
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