ArticleProceedings of the National Academy of Sciences of the United States of America1999
Novel mechanisms control the folding and assembly of lambda5/14.1 and VpreB to produce an intact surrogate light chain.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 54 citations in OpenAlex.
- Association-induced folding governs surrogate light chain and pre-B cell receptor core assembly.Nature communications · 2026Article
- Evolution of surrogate light chain in tetrapods and the relationship between lengths of CDR H3 and VpreB tails.Frontiers in immunology · 2022Article
- The Role of the Pre-B Cell Receptor in B Cell Development, Repertoire Selection, and Tolerance.Frontiers in immunology · 2018Review
- The Sel1L-Hrd1 Endoplasmic Reticulum-Associated Degradation Complex Manages a Key Checkpoint in B Cell Development.Cell reports · 2016Article
- Dimerization-dependent folding underlies assembly control of the clonotypic αβT cell receptor chains.The Journal of biological chemistry · 2015Article
- N-linked glycosylation selectively regulates autonomous precursor BCR function.Nature immunology · 2010Article
- Engineering and characterization of a single chain surrogate light chain variable domain.Protein science : a publication of the Protein Society · 2008Article
- Variable domains and a VpreB-like molecule are present in a jawless vertebrate.Immunogenetics · 2005Article
- Fit for life in the immune system? Surrogate L chain tests H chains that test L chains.Proceedings of the National Academy of Sciences of the United States of America · 1999Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Surrogate light chain, which escorts the mu heavy chain to the cell surface, is a critical component of the pre-B cell receptor complex. The two proteins that comprise the surrogate light chain, VpreB and lambda5/14.1, contain both unique regions and Ig-like domains. The unique regions have been postulated to function in the assembly of the surrogate light chain. However, by using transient transfection of COS7 cells, we show that deletion of the unique regions of both proteins did not inhibit the assembly of surrogate light chain. Instead, in vivo folding studies showed that the unique region of lambda5/14.1 acts as an intramolecular chaperone by preventing the folding of this protein when it is expressed in the absence of its partner, VpreB. The Ig domains of both lambda5/14.1 and VpreB are atypical. The one in VpreB lacks one of the canonical beta strands whereas the one in lambda5/14.1 has an extra beta strand. Deletion of the extra beta strand in lambda5/14.1 completely abrogated the formation of the surrogate light chain, demonstrating that complementation of the incomplete Ig domain in VpreB by the extra beta strand in lambda5/14.1 was necessary and sufficient for the folding and assembly of these proteins. Our studies reveal two novel mechanisms for regulating surrogate light chain formation: (i) the presence of an intramolecular chaperone that prevents folding of the unassembled subunit but that remains part of the mature assembled protein, and (ii) splitting an Ig domain between two proteins to control their folding and assembly.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.