RIAM Regulates the Cytoskeletal Distribution and Activation of PLC-γ1 in T Cells

Nikolaos Patsoukis, Esther M. Lafuente, Paul Meraner, Jin sub Kim, David Dombkowski, Lequn Li, Vassiliki A. Boussiotis*

*To whom correspondence should be addressed. E-mail: vboussio{at}bidmc.harvard.edu

This PDF file includes:

• Fig. S1. Colocalization of RIAM with ZAP-70 and F-actin at the IS.
• Fig. S2. Reduced abundance of RIAM in RIAM-KD Jurkat T cell lines.
• Fig. S3. Effects of knockdown of RIAM on Ca²⁺ mobilization.
• Fig. S4. The interaction between PLC-γ1 and RIAM requires the C-terminal PRR of RIAM.
• Fig. S5. Reconstitution of RIAM-KD cells with RIAM-D1 does not restore their ability to activate MEK, ERK, or JNK.
• Fig. S6. Negative controls used in detecting the colocalization of phosphorylated PLC-γ1 and F-actin.
• Fig. S7. Negative controls used in detecting colocalization of PIP₂ with the actin cytoskeleton.
• Fig. S8. RIAM and LAT associate with separate pools of PLC-γ1.
• Fig. S9. Knockdown of RIAM does not affect the abundance of pLAT.
• Fig. S10. Analysis of the purity of cytoskeletal fractions.

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© 2009 American Association for the Advancement of Science