Supplementary Materials
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).