Evidence map›Paper›PMID 19372136›Full record

ArticleMolecular & cellular proteomics : MCP2009

SLP-65 phosphorylation dynamics reveals a functional basis for signal integration by receptor-proximal adaptor proteins.

Thomas Oellerich, Mads Grønborg, Konstantin Neumann, He-Hsuan Hsiao, Henning Urlaub, Jürgen Wienands

Abstract read
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Article in Molecular & cellular proteomics : MCP, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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3 · Its place in the literature

Who cites it

17 citing papers in PubMed.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors.

Thomas OellerichInstitute of Cellular and Molecular Immunology, Georg August University of Göttingen, Göttingen, Germany.
Mads Grønborg
Konstantin Neumann
He-Hsuan Hsiao
Henning Urlaub
Jürgen Wienands

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Understanding intracellular signal transduction by cell surface receptors requires information about the precise order of relevant modifications on the early transducer elements. Here we introduce the B cell line DT40 and its genetically engineered variants as a model system to determine and functionally characterize post-translational protein modifications in general. This is accomplished by a customized strategy that combines mass spectrometric analyses of protein modifications with subsequent mutational studies. When applied to the B cell receptor (BCR)-proximal effector SLP-65, this approach uncovered a differential and highly dynamic engagement of numerous newly identified phospho-acceptor sites. Some of them serve as kinase substrates in resting cells and undergo rapid dephosphorylation upon BCR ligation. Stimulation-induced phosphorylation of SLP-65 can be early and transient, or early and sustained, or late. Functional elucidation of conspicuous phosphorylation at serine 170 in SLP-65 revealed a BCR-distal checkpoint for some but not all possible B cell responses. Our data show that SLP-65 phosphorylation acts upstream for signal initiation and also downstream during selective processing of the BCR signal. Such a phenomenon defines a receptor-specific signal integrator.

Indexed as

Adaptor Proteins, Signal TransducingAmino Acid SequenceAnimalsB-LymphocytesCell LineChickensMitogen-Activated Protein KinasesMolecular Sequence DataPeptidesPhosphorylationReceptors, Antigen, B-CellReceptors, Cell SurfaceRecombinant Fusion ProteinsSignal TransductionAdaptor Proteins, Signal TransducingB cell linker proteinMitogen-Activated Protein KinasesPeptidesReceptors, Antigen, B-CellReceptors, Cell SurfaceRecombinant Fusion Proteins

Identifiers

PMID19372136
PMCPMC2709198

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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.