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Structural basis for galectin-1-dependent pre-B cell receptor (pre-BCR) activation.

Abstract : During B cell differentiation in the bone marrow, the expression and activation of the pre-B cell receptor (pre-BCR) constitute crucial checkpoints for B cell development. Both constitutive and ligand-dependent pre-BCR activation modes have been described. The pre-BCR constitutes an immunoglobulin heavy chain (Ig?) and a surrogate light chain composed of the invariant ?5 and VpreB proteins. We previously showed that galectin-1 (GAL1), produced by bone marrow stromal cells, is a pre-BCR ligand that induces receptor clustering, leading to efficient pre-BII cell proliferation and differentiation. GAL1 interacts with the pre-BCR via the unique region of ?5 (?5-UR). Here, we investigated the solution structure of a minimal ?5-UR motif that interacts with GAL1. This motif adopts a stable helical conformation that docks onto a GAL1 hydrophobic surface adjacent to its carbohydrate binding site. We identified key hydrophobic residues from the ?5-UR as crucial for the interaction with GAL1 and for pre-BCR clustering. These residues involved in GAL1-induced pre-BCR activation are different from those essential for autonomous receptor activation. Overall, our results indicate that constitutive and ligand-induced pre-BCR activation could occur in a complementary manner.
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https://hal.archives-ouvertes.fr/hal-01458259
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Submitted on : Thursday, May 27, 2021 - 10:00:56 AM
Last modification on : Friday, May 6, 2022 - 2:56:02 PM
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Latifa El Antak, Marion Espeli, Annie Boned, Olivier Bornet, Jeremy Bonzi, et al.. Structural basis for galectin-1-dependent pre-B cell receptor (pre-BCR) activation.. Journal of Biological Chemistry, American Society for Biochemistry and Molecular Biology, 2012, 287 (53), pp.44703--13. ⟨10.1074/jbc.M112.395152⟩. ⟨hal-01458259⟩

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