Unknown

Dataset Information

0

Galectin-1 is a stromal cell ligand of the pre-B cell receptor (BCR) implicated in synapse formation between pre-B and stromal cells and in pre-BCR triggering.


ABSTRACT: Although preB cell-receptor (pre-BCR) formation and cell-surface expression is essential for B cell development, pre-BCR generation of signal transduction remains elusive. Here, we report that recombinant pre-BCRs and the surrogate light chain bind specifically to the bone marrow stromal cell galectin-1 (GAL1), an S-type lectin. The surrogate light chain/GAL1 association is a direct protein-protein interaction (K(a) = 2 x 10(6) M(-1)), and the NH(2) extra loop of lambda-like is the major binding element. Pre-BCR binding to stromal cells depends upon GAL1 anchoring to glycosylated counter-receptors, and these complexes completely relocalize to form a synapse at the contact zone between preB and stromal cells. This immune developmental synapse is accompanied by the initiation of intracellular tyrosine kinase activity and signal transduction from the pre-BCR.

SUBMITTER: Gauthier L 

PROVIDER: S-EPMC130578 | biostudies-literature | 2002 Oct

REPOSITORIES: biostudies-literature

altmetric image

Publications

Galectin-1 is a stromal cell ligand of the pre-B cell receptor (BCR) implicated in synapse formation between pre-B and stromal cells and in pre-BCR triggering.

Gauthier Laurent L   Rossi Benjamin B   Roux Florence F   Termine Elise E   Schiff Claudine C  

Proceedings of the National Academy of Sciences of the United States of America 20020923 20


Although preB cell-receptor (pre-BCR) formation and cell-surface expression is essential for B cell development, pre-BCR generation of signal transduction remains elusive. Here, we report that recombinant pre-BCRs and the surrogate light chain bind specifically to the bone marrow stromal cell galectin-1 (GAL1), an S-type lectin. The surrogate light chain/GAL1 association is a direct protein-protein interaction (K(a) = 2 x 10(6) M(-1)), and the NH(2) extra loop of lambda-like is the major binding  ...[more]

Similar Datasets

| S-EPMC3531785 | biostudies-literature
| S-EPMC3284572 | biostudies-literature
| S-EPMC6098130 | biostudies-literature
| S-EPMC2829314 | biostudies-literature
| S-EPMC2643495 | biostudies-literature
| S-EPMC2722676 | biostudies-literature
| S-EPMC2732795 | biostudies-literature
| S-EPMC3672982 | biostudies-literature