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

Oellerich, T., Grønborg, M., Neumann, K., Hsiao, H. H., Urlaub, H., & Wienands, J. (2009). SLP-65 phosphorylation dynamics reveals a functional basis for signal integration by receptor-proximal adaptor proteins. Molecular and Cellular Proteomics, 8(7), 1738-1750. doi:10.1074/mcp.M800567-MCP200.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0010-9352-D Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-F25C-B
Genre: Journal Article

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 Creators:
Oellerich, T., Author
Grønborg, M.1, Author              
Neumann, K., Author
Hsiao, H. H.2, Author              
Urlaub, H.2, Author              
Wienands, J., Author
Affiliations:
1Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society, ou_578595              
2Research Group of Bioanalytical Mass Spectrometry, MPI for biophysical chemistry, Max Planck Society, ou_578613              

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 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. Stimulationinduced 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.

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Language(s): eng - English
 Dates: 2009-04-162009-07
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: eDoc: 434354
DOI: 10.1074/mcp.M800567-MCP200
 Degree: -

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Title: Molecular and Cellular Proteomics
Source Genre: Journal
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Pages: - Volume / Issue: 8 (7) Sequence Number: - Start / End Page: 1738 - 1750 Identifier: -