Supplementary Materials for:

Association of the EF-hand and PH domains of the guanine nucleotide exchange factor SLAT with IP₃ receptor 1 promotes Ca²⁺ signaling in T cells

Camille Fos, Stephane Becart, Ann J. Canonigo Balancio, Darren Boehning, Amnon Altman*

*Corresponding author. E-mail: amnon{at}liai.org

This PDF file includes:

• Fig. S1. The SLAT-IP₃R1 interaction is direct.
• Fig. S2. Binding of the EF-hand and PH domains of SLAT to IP₃R1.
• Fig. S3. Critical role of a conserved 18–amino acid motif in the IP₃R1 ligand-binding domain for its interaction with SLAT.
• Fig. S4. The abundance of IP₃R1 in T cells is unaffected by loss of SLAT.
• Fig. S5. Effects of disrupting the SLAT-IP₃R1 interaction on Ca²⁺ release from intracellular stores, TCR-proximal signaling, and NF-κB activity.
• Fig. S6. Hypothetical model of the Ca²⁺-SLAT-IP₃R1 interaction.
• Reference (44)

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Citation: C. Fos, S. Becart, A. J. C. Balancio, D. Boehning, A. Altman, Association of the EF-hand and PH domains of the guanine nucleotide exchange factor SLAT with IP₃ receptor 1 promotes Ca²⁺ signaling in T cells. Sci. Signal. 7, ra93 (2014).

© 2014 American Association for the Advancement of Science