|
||
Journal of Experimental Medicine, Vol 176, 1025-1031, Copyright © 1992 by Rockefeller University Press
ARTICLES |
VS Parikh, GA Bishop, KJ Liu, BT Do, MR Ghosh, BS Kim and PW Tucker
Department of Microbiology, University of Texas Southwestern Medical Center, Dallas 75235.
By generating phosphorylcholine (PC)-specific, wild-type (mu), and chimeric (mu-I-A alpha) antigen receptor transfectants of mature B cells, we have shown that the COOH terminus of the mu heavy chain is essential for three major functions: immediate signal transduction (measured as changes in intracellular Ca2+), antigen presentation, and induction of immunoglobulin M secretion. A more detailed analysis of structural requirements of the COOH-terminal domains contributing to these functions was achieved by systematically replacing the spacer, cytoplasmic, and transmembranal domains of the mu-I-A alpha chimeric chain with those of mu. Using this rescue approach, we show that the carboxyl two-thirds of the transmembranal domain (proximal to the cytoplasmic domain) is required for induction of intracellular Ca2+, whereas the complete transmembranal domain is required for the function of antigen presentation but is dispensable for induction of antibody secretion.
This article has been cited by other articles:
| TABLE OF CONTENTS |
|