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Updated: Aug 16, 2026

Examining BCL-2 Family Function with Large Unilamellar Vesicles
Published on: October 5, 2012
Regulation of Bcl-3 through interaction with the Lck tyrosine kinase
Yujie Zhao1, Aravind Ramakrishnan, Kyoung-Eun Kim
1Center for Advanced Biotechnology and Medicine, University of Medicine and Dentistry of New Jersey, Robert Wood Johnson Medical School, Piscataway, NJ 08854, USA.
Abstract:
bcl-3 is a protooncogene which undergoes chromosomal translocation in a subset of chronic B-cell lymphocytic leukemia cells. Bcl-3 is a unique IkappaB family protein that regulates transcription of a number of NF-kappaB target genes through interactions with NF-kappaB dimers. Based on previous studies, suggesting that Bcl-3 interacts with the Fyn tyrosine kinase in platelets, we investigated possible interactions of Bcl-3 with Lck, a related tyrosine kinase important in lymphoid cells. Protein-protein interactions between Bcl-3 and the Lck tyrosine kinase were identified both in vitro and in vivo. Lck enhanced Bcl-3-mediated activation of a p52/Bcl-3-responsive promoter in reporter gene assays independent of its tyrosine kinase activity, but requiring the Lck SH3 protein interaction domain. These studies suggest that Bcl-3 might participate in oncogenic pathways involving Lck.
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