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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© 2012 American Association for the Advancement of Science