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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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
