Supplementary Materials

Supplementary Materials for:

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

Michael Engelke, Sona Pirkuliyeva, Julius Kühn, Leo Wong, Janina Boyken, Nadine Herrmann, Stefan Becker, Christian Griesinger, Jürgen Wienands*

*Corresponding author. E-mail: jwienan@gwdg.de

This PDF file includes:

  • Fig. S1. The N terminus of SLP-65 is essential for the BCR-dependent activation of ERK.
  • Fig. S2. Differently tagged SLP-65 forms do not coimmunoprecipitate with each other.
  • Fig. S3. SLP-65 associates with membranes in resting human B cells.
  • Fig. S4. The L18K variant of SLP-65 cannot signal.
  • Fig. S5. The N terminus of SLP-65 is intrinsically disordered in solution and binds directly to liposomes.
  • Fig. S6. Inactivation of the putative leucine zipper motif only marginally affects BCR-induced Ca2+ mobilization.
  • Fig. S7. Lack of colocalization between SLP-65 and syntaxin 8 and SNAP23.
  • Fig. S8. N terminus–dependent attachment of SLP-65 to VAMP7-positive vesicles as revealed by bimolecular fluorescence complementation experiments.
  • Fig. S9. The vesicle-associated and cytosolic SLP-65 pools exchange rapidly with each other.
  • Fig. S10. The OSBP1-PH domain is insufficient to target chimeric SLP-65 protein to VAMP7-positive vesicles.

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Citation: M. Engelke, S. Pirkuliyeva, J. Kühn, L. Wong, J. Boyken, N. Herrmann, S. Becker, C. Griesinger, J. Wienands, Macromolecular assembly of the adaptor SLP-65 at intracellular vesicles in resting B cells. Sci. Signal. 7, ra79 (2014).

© 2014 American Association for the Advancement of Science