Abstract
The B cell receptor for antigen, the membrane immunoglobulin (mIg) molecule, is normally expressed in association with at least two other proteins, mb-1 (Ig-α) and B29 (Ig-β/γ). We have previously described a set of murine B cell clones transfected with wild-type and mutated forms of membrane-bound IgM (mIgM) that vary in their ability to transduce signals to the cell interior. Analysis of the B cell receptor complex in signaling and nonsignaling mutants of mIgM reveals complete concordance between intact signaling ability and ability of the mIgM to associate with Ig-α and Ig-β/γ. These results point to the importance of the mIgM transmembrane region in mediating binding to accessory molecules, and provide support for a role of Ig-α and Ig-β/γ that extends beyond surface expression to signal transduction in B lymphocytes.
| Original language | English |
|---|---|
| Pages (from-to) | 25776-25779 |
| Number of pages | 4 |
| Journal | Journal of Biological Chemistry |
| Volume | 268 |
| Issue number | 34 |
| State | Published - Dec 5 1993 |
Keywords
- Amino Acid Sequence
- Animals
- Antigens, CD
- B-Lymphocytes/immunology
- Blotting, Western
- CD79 Antigens
- Calcium/metabolism
- Cell Line
- Humans
- Immunoglobulin G/biosynthesis
- Immunoglobulin M/biosynthesis
- Lymphoma, B-Cell
- Membrane Glycoproteins/isolation & purification
- Mice
- Molecular Sequence Data
- Mutagenesis
- Phosphoproteins/isolation & purification
- Protein Kinases/metabolism
- Receptors, Antigen, B-Cell/genetics
- Signal Transduction/genetics
- Transfection
- Tumor Cells, Cultured