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Sci. Signal., 31 July 2012
[DOI: 10.1126/scisignal.2002820]

Supplementary Materials for:

The Scaffolding Protein Synapse-Associated Protein 97 Is Required for Enhanced Signaling Through Isotype-Switched IgG Memory B Cell Receptors

Wanli Liu, Elizabeth Chen, Xing Wang Zhao, Zheng Peng Wan, Yi Ren Gao, Angel Davey, Eric Huang, Lijia Zhang, Jillian Crocetti, Gabriel Sandoval, M. Gordon Joyce, Carrie Miceli, Jan Lukszo, L. Aravind, Wojciech Swat, Joseph Brzostowski, Susan K. Pierce*

*To whom correspondence should be addressed. E-mail: spierce{at}nih.gov

This PDF file includes:

  • Fig. S1. The cytoplasmic tail of mIgG binds to SAP97.
  • Fig. S2. SAP97 is the most abundant SAP family protein in B cells.
  • Fig. S3. Knockdown of SAP97 has mild effects on antigen-induced accumulation of IgM BCRs in the immunological synapse.
  • Fig. S4. The extent of colocalization of IgG-SSVV/AAAA mutant BCRs with SAP97 upon antigen engagement is substantially reduced compared to that of IgG-WT BCRs.
  • Movies S1 to S4 captions

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Size: 343 KB

Other Supplementary Material for this manuscript includes the following:

  • Movies S1 to S4 (.avi format)

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Citation: W. Liu, E. Chen, X. W. Zhao, Z. P. Wan, Y. R. Gao, A. Davey, E. Huang, L. Zhang, J. Crocetti, G. Sandoval, M. G. Joyce, C. Miceli, J. Lukszo, L. Aravind, W. Swat, J. Brzostowski, S. K. Pierce, The Scaffolding Protein Synapse-Associated Protein 97 Is Required for Enhanced Signaling Through Isotype-Switched IgG Memory B Cell Receptors. Sci. Signal. 5, ra54 (2012).

© 2012 American Association for the Advancement of Science


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