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Role of the extracellular and transmembrane domain of Ig-alpha/beta in assembly of the B cell antigen receptor (BCR). | LitMetric

Role of the extracellular and transmembrane domain of Ig-alpha/beta in assembly of the B cell antigen receptor (BCR).

Immunol Lett

Cell Biology Group, Department of Zoology, University of British Columbia, 2350 Health Sciences Mall, Vancouver, BC V6T 1Z3, Canada.

Published: September 2007

AI Article Synopsis

  • - The B cell antigen receptor (BCR) is crucial for B-lymphocyte function, consisting of membrane IgM and two signaling proteins, Ig-alpha and Ig-beta, which are essential for its transportation to the cell surface and effective signaling.
  • - Successful assembly and proper cell surface expression of the BCR depend on specific protein interactions between the extracellular and transmembrane regions of Ig-alpha and Ig-beta.
  • - Mutations in Ig-alpha that disrupt its ability to interact with Ig-beta hinder BCR assembly, while specific modifications allowing proper interaction can restore functionality, highlighting the importance of these regions for B cell development.

Article Abstract

The B cell antigen receptor (BCR) is expressed on the surface of B-lymphocytes where it binds antigen and transmits signals that regulate B cell activation, growth and differentiation. The BCR is composed of membrane IgM (mIgM) and two signaling proteins, Ig-alpha and Ig-beta. If either of the signaling proteins is not expressed, the incomplete mIgM-containing BCR will not traffic to the cell surface. Our hypothesis is that specific protein:protein interactions between both the extracellular and transmembrane (TM) regions of Ig-alpha and Ig-beta are necessary for receptor assembly, cell surface expression and effective signaling to support the proper development of B cells. While previous work has shown the importance of the TM region in BCR assembly, this study indicates that a heterodimer of the extracellular domains of Ig-alpha and Ig-beta are also required for proper association with mIgM. Cell lines expressing mutated Ig-alpha proteins that did not heterodimerize with Ig-beta in the extracellular and TM domains were unable to properly assemble the BCR. Conversely, an Ig-alpha mutant with an Ig-beta cytoplasmic tail (Cbeta (alpha/alpha/beta)) was able to assemble with the rest of the BCR, in particular with Ig-beta, and traffic to the cell surface. Thus, both the extracellular and TM regions of the Ig-alpha/Ig-beta must be properly associated in order for the BCR to assemble.

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Source
http://dx.doi.org/10.1016/j.imlet.2007.06.005DOI Listing

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