Table 2.
Some cellular proteins containing a lipid/protein interaction domain were identified as PI5P binding partners.
| Binding domain | PI binding | Experiment used | Protein role | Reference |
|---|---|---|---|---|
| CYTOSOL, PLASMA MEMBRANE | ||||
| PH Dok-1/Dok-2 | PI4P, PI5P | Fat blot, SPR | Negative regulation T cell signaling | Guittard et al. (2009) |
| PH-Dok-4 | PI5P > Mono-PIs | Fat blot, SPR | Negative/positive regulation T cell signaling | Guittard et al. (2010) |
| PH Dok-5 | PI5P+++ | Fat blot, SPR | Cardiomyocyte differentiation PI3K depdt | Guittard et al. (2010) |
| BIN1 | PI5P, PI3P | SPR | Tubular invaginations of membranes, biogenesis of muscle T tubules | Nicot et al. (2007), Fugier et al. (2011) |
| NUCLEUS | ||||
| ATX-1-PHD | PI5P+++ | Fat blot | Plant (Arapidopsis thaliana) chromatin modification stress induced | Alvarez-Venegas et al. (2006) |
| ING2 PHD | PI5P+, PI3P | Fat blot, SPR, PIP-beads | Nucleus cellular stress response | Gozani et al. (2003) |
| Sap30L/Sap 30 | PI5P > PI3P > PI4 | Fat blot | Chromatin remodeling, transcription | Viiri et al. (2009) |
| PH-tfb1 TFII subunit | PI5P, PI3P | Fat blot | Transcription factor | Di Lello et al. (2005) |
Different experimental approaches were used to characterize this PI5P binding. These proteins are expressed in different subcellular compartments and are involved in different cell functions. PH, Pleckstrin homology domain; PHD, plant homeo-domain; SPR, surface plasmon resonance.