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  Macromolecular assembly of the adaptor SLP-65 at intracellular vesicles in resting B cells.

Engelke, M., Pirkuliyeva, S., Kühn, J., Wong, L., Boyken, J., Hermann, N., et al. (2014). Macromolecular assembly of the adaptor SLP-65 at intracellular vesicles in resting B cells. Science Signaling, 7(339): ra79. doi:10.1126/scitranslmed.2005104.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0023-E08E-D Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-2C49-A
Genre: Journal Article

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 Creators:
Engelke, M., Author
Pirkuliyeva, S., Author
Kühn, J., Author
Wong, L., Author
Boyken, J.1, Author              
Hermann, N., Author
Becker, S.2, Author              
Griesinger, C.2, Author              
Wienands, J., Author
Affiliations:
1Department of Neurobiology, MPI for biophysical chemistry, Max Planck Society, ou_578595              
2Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              

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 Abstract: The traditional view of how intracellular effector proteins are recruited to the B cell antigen receptor (BCR) complex at the plasma membrane is based on the occurrence of direct protein-protein interactions, as exemplified by the recruitment of the tyrosine kinase Syk (spleen tyrosine kinase) to phosphorylated motifs in BCR signaling subunits. By contrast, the subcellular targeting of the cytosolic adaptor protein SLP-65 (Src homology 2 domain-containing leukocyte adaptor protein of 65 kD), which serves as a proximal Syk substrate, is unclear. We showed that SLP-65 activation required its association at vesicular compartments in resting B cells. A module of similar to 50 amino acid residues located at the amino terminus of SLP-65 anchored SLP-65 to the vesicles. Nuclear magnetic resonance spectroscopy showed that the SLP-65 amino terminus was structurally disordered in solution, but could bind in a structured manner to noncharged lipid components of cellular membranes. Our finding that preformed vesicular signaling scaffolds are required for B cell activation indicates that vesicles may deliver preassembled signaling cargo to sites of BCR activation.

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Language(s): eng - English
 Dates: 2014-08-19
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1126/scitranslmed.2005104
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Title: Science Signaling
Source Genre: Journal
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Pages: 8 Volume / Issue: 7 (339) Sequence Number: ra79 Start / End Page: - Identifier: -