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The nonimmunoglobulin portion of lambda5 mediates cell-autonomous pre-B cell receptor signaling.

Abstract：

:The pre-B cell receptor (preBCR), composed of mu immunoglobulin (Ig) and surrogate light chains, signals large 'preB-II' cells to proliferate in the apparent absence of ligands or cooperating cells. We deleted the N-terminal, nonimmunoglobulin (nonlg) portion of lambda5, or mutated seven arginine residues in it to serine residues. PreBCRs with such mutant lambda5 proteins showed increased cell surface representation and a diminished rate of aggregation and internalization. Tyrosine phosphorylation of preBCR complexes containing mutant lambda5 proteins was abolished. These results indicate that the nonIg portion of lambda5, and the seven arginine residues in it, are needed for signal transduction, and that signaling could be cell autonomous. We propose two models to explain the apparently constitutive, ligand-independent signal-transducing capacity of the preBCR.

journal_name

Nat Immunol

journal_title

Nature immunology

authors

Ohnishi K,Melchers F

doi

10.1038/ni959

keywords:

subject

Has Abstract

pub_date

2003-09-01 00:00:00

pages

849-56

issue

9

eissn

1529-2908

issn

1529-2916

pii

ni959

journal_volume

4

pub_type

杂志文章

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