Role of the extracellular and transmembrane domain of Ig-α/β in assembly of the B cell antigen receptor (BCR)

2007 ◽  
Vol 112 (1) ◽  
pp. 47-57 ◽  
Author(s):  
Janis Dylke ◽  
Jared Lopes ◽  
May Dang-Lawson ◽  
Steve Machtaler ◽  
Linda Matsuuchi
Keyword(s):  
B Cell ◽  
Transmembrane Domain ◽  
Antigen Receptor ◽  
B Cell Antigen Receptor ◽  
Cell Antigen Receptor ◽  
Cell Antigen

The role of Ig-α/β in B cell antigen receptor internalization

2010 ◽  
Vol 134 (1) ◽  
pp. 75-82 ◽  
Author(s):  
Caren Jang ◽  
Steven Machtaler ◽  
Linda Matsuuchi
Keyword(s):  
B Cell ◽  
Antigen Receptor ◽  
Receptor Internalization ◽  
B Cell Antigen Receptor ◽  
Cell Antigen Receptor ◽  
Cell Antigen

scholarly journals A symmetric geometry of transmembrane domains inside the B cell antigen receptor complex

2019 ◽  
Vol 116 (27) ◽  
pp. 13468-13473 ◽  
Author(s):  
Cornelia Gottwick ◽  
Xiaocui He ◽  
Andreas Hofmann ◽  
Niklas Vesper ◽  
Michael Reth ◽  
...  
Keyword(s):  
B Cell ◽  
Transmembrane Domain ◽  
Mutational Analysis ◽  
Antigen Receptor ◽  
B Cell Antigen Receptor ◽  
Cell Antigen Receptor ◽  
Cell Antigen ◽  
Symmetric Complex ◽  
Multiple Copies ◽  
Membrane Bound

B lymphocytes have the ability to sense thousands of structurally different antigens and produce cognate antibodies against these molecules. For this they carry on their surface multiple copies of the B cell antigen receptor (BCR) comprising the membrane-bound Ig (mIg) molecule and the Igα/Igβ heterodimer functioning as antigen binding and signal transducing components, respectively. The mIg is a symmetric complex of 2 identical membrane-bound heavy chains (mHC) and 2 identical light chains. How the symmetric mIg molecule is asymmetrically associated with only one Igα/Igβ heterodimer has been a puzzle. Here we describe that Igα and Igβ both carry on one side of their α-helical transmembrane domain a conserved amino acid motif. By a mutational analysis in combination with a BCR rebuilding approach, we show that this motif is required for the retention of unassembled Igα or Igβ molecules inside the endoplasmic reticulum and the binding of the Igα/Igβ heterodimer to the mIg molecule. We suggest that the BCR forms within the lipid bilayer of the membrane a symmetric Igα-mHC:mHC-Igβ complex that is stabilized by an aromatic proline-tyrosine interaction. Outside the membrane this symmetry is broken by the disulfide-bridged dimerization of the extracellular Ig domains of Igα and Igβ. However, symmetry of the receptor can be regained by a dimerization of 2 BCR complexes as suggested by the dissociation activation model.

scholarly journals Role of B-cell antigen receptor-associated molecules and lipid rafts in CD5-induced apoptosis of B CLL cells

Leukemia ◽  
2004 ◽  
Vol 19 (2) ◽  
pp. 223-229 ◽  
Author(s):  
Y Renaudineau ◽  
S Nédellec ◽  
C Berthou ◽  
P M Lydyard ◽  
P Youinou ◽  
...  
Keyword(s):  
B Cell ◽  
Lipid Rafts ◽  
Antigen Receptor ◽  
B Cell Antigen Receptor ◽  
Cell Antigen Receptor ◽  
Cell Antigen ◽  
Induced Apoptosis
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