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Cited by 271T-cell and B-cell ImmunologyNF-κB Signaling PathwaysProtein Kinase Regulation and GTPase Signaling

SLP-65: A New Signaling Component in B Lymphocytes which Requires Expression of the Antigen Receptor for Phosphorylation

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Wienands, Jürgen, Schweikert, Jutta, Wollscheid, Bernd, Jumaa, Hassan, Nielsen, Peter J., Reth, Michael·1998·The Journal of Experimental Medicine
DOI 10.1084/jem.188.4.791PMC PMC2213353
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Abstract

The B cell antigen receptor (BCR) consists of the membrane-bound immunoglobulin (Ig) molecule as antigen-binding subunit and the Ig-α/Ig-β heterodimer as signaling subunit. BCR signal transduction involves activation of protein tyrosine kinases (PTKs) and phosphorylation of several proteins, only some of which have been identified. The phosphorylation of these proteins can be induced by exposure of B cells either to antigen or to the tyrosine phosphatase inhibitor pervanadate/H2O2. One of the earliest substrates in B cells is a 65-kD protein, which we identify here as a B cell adaptor protein. This protein, named SLP-65, is part of a signaling complex involving Grb-2 and Vav and shows homology to SLP-76, a signaling element of the T cell receptor. In pervanadate/H2O2-stimulated cells, SLP-65 becomes phosphorylated only upon expression of the BCR. These data suggest that SLP-65 is part of a BCR transducer complex.

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  • Several elements of the canonical BCR signaling cascade, e.g. Syk, Btk, and BLNK, are known to physically interact with and activate the Rac activator Vav, by processes not necessarily involving the protein kinase activity of Btk.

    “Thus, several elements of the canonical BCR signaling cascade, e.g.Syk (50), Btk (51), and BLNK (52,53), are known to physically interact with and activate the Rac activator Vav, by processes not necessarily involving the protein kinase activity of Btk.”

    From The Phospholipase Cγ2 Mutants R665W and L845F Identified in Ibrutinib-resistant Chronic Lymphocytic Leukemia Patients Are Hypersensitive to the Rho GTPase Rac2 Protein (2016) · cites this paper as [53]

    The Results and Discussion (page not provided) report that SLP-65 coprecipitates with Vav and is constitutively associated with it, supporting the physical-interaction part of the BLNK citation. The paper does not show that SLP-65 activates Vav. The separate claim about Btk kinase activity is attached to the Btk citation, not specifically to this source. (LLM, conf=0.86)

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Cites

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Research works printed but not linked: 26

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Cited by

Sorted by citations

Authors
Wienands, J., Schweikert, J., Wollscheid, B., Jumaa, H., Nielsen, P. J., & Reth, M.
Affiliations
Max Planck Society (DE)
ORCID
Venue
The Journal of Experimental Medicine
Publisher
Rockefeller University Press
Published
1998-08-17
Volume
188
Issue
4
Pages
791-795
ISSN
  • 0022-1007 (ISSN-L)
  • 1540-9538
DOI
10.1084/jem.188.4.791
PMC
PMC2213353
OpenAlex
W2009818164
Cited by
271
References
0
Citations by year
2025: 1 · 2024: 4 · 2023: 3 · 2022: 4 · 2020: 5 · 2019: 2 · 2018: 10 · 2017: 6 · 2016: 8 · 2015: 7 · 2014: 7 · 2013: 6 · 2012: 7
FWCI
10.20
Type
journal article
Language
en
Open access
Locations
  • The Journal of Experimental Medicine (publishedVersion)
  • PubMed Central (publishedVersion, cc-by-nc-sa)
  • PubMed (publishedVersion)
  • Bayerische Staatsbibliothek (submittedVersion)
Topics
  • Life Sciences › Immunology and Microbiology › Immunology › T-cell and B-cell Immunology
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Keywords
B cell receptor, B cells, signal transduction, protein phosphorylation, Grb2, Vav, SLP-76, adaptor proteins, tyrosine kinase, T cell receptor signaling
MeSH terms
Amino Acid Sequence, Animals, B-Lymphocytes, Base Sequence, Carrier Proteins, Enzyme Inhibitors, Humans, Hydrogen Peroxide, Immunoglobulin delta-Chains, Immunoglobulin mu-Chains, Molecular Sequence Data, Phosphoproteins, Protein-Tyrosine Kinases, Proteins, Proto-Oncogene Proteins, Rabbits, Receptors, Antigen, B-Cell, Tumor Cells, Cultured, Vanadates, Signal Transduction, DNA, Complementary, Cell Cycle Proteins, Adaptor Proteins, Signal Transducing, GRB2 Adaptor Protein, Proto-Oncogene Proteins c-vav

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