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Sci. Signal., 18 December 2012
[DOI: 10.1126/scisignal.2003289]

Supplementary Materials for:

A CC-SAM, for Coiled Coil–Sterile α Motif, Domain Targets the Scaffold KSR-1 to Specific Sites in the Plasma Membrane

Dorothy Koveal, Natasha Schuh-Nuhfer, Daniel Ritt, Rebecca Page, Deborah K. Morrison,* Wolfgang Peti*

*To whom correspondence should be addressed. E-mail: morrisod{at}mail.nih.gov (D.K.M.); Wolfgang_Peti{at}brown.edu (W.P.)

This PDF file includes:

  • Fig. S1. Comparison of abundance of wild-type KSR-1 and ΔN170–KSR-1.
  • Fig. S2. Cellular localization of wild-type or mutant KSR-1 proteins upon stimulation with EGF.
  • Fig. S3. Characterization of the CC-SAM domain.
  • Fig. S4. Structural homologs of the KSR-1 SAM domain.
  • Fig. S5. The CC-SAM domain is a single, structured domain.
  • Fig. S6. Interactions made by Leu56 and Arg57.
  • Fig. S7. The CC-SAM domain does not bind RNA- or KSR-1–interacting proteins.
  • Fig. S8. The KSR-1 CC-SAM domain binds directly to SDS micelles.
  • Fig. S9. CC-SAM interacts similarly with SDS micelles and LMPG micelles.
  • Fig. S10. CC-SAM residues Ile71 and Leu78 mediate membrane binding.
  • Table S1. Residues involved in membrane binding and domain stability.
  • Table S2. CC-SAM is not a protein interaction domain.

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Technical Details

Format: Adobe Acrobat PDF

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Citation: D. Koveal, N. Schuh-Nuhfer, D. Ritt, R. Page, D. K. Morrison, W. Peti, A CC-SAM, for Coiled Coil–Sterile α Motif, Domain Targets the Scaffold KSR-1 to Specific Sites in the Plasma Membrane. Sci. Signal. 5, ra94 (2012).

© 2012 American Association for the Advancement of Science


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