Table 1.
Protein 4.1B/DAL-1-interacting molecules
| Molecules | Characteristics | Binding domain | Functions of binding protein-4.1B/DAL-1 complex | Note | References |
|---|---|---|---|---|---|
| Spectrin, actin | The cytoskeleton | SABD | Provides cytoskeletal linkage and modulates important cytoskeletal functions in a wide variety of cells and tissues | 1, 2 | [42] |
| 14-3-3 proteins | Adapter proteins | FERM | Not determined | 3, 4, 5, 6 | [43] |
| Caspr/paranodin, Caspr2 | Neuronal transmembrane glycoprotein | FERM | At paranodes and juxtaparanodes, 4.1B associates with Caspr/paranodin and Caspr2, respectively, and anchors them to the axonal cytoskeleton | 5, 6, 7 | [30] |
| pICln | Swelling-activated anion channel | FERM | Participating in the regulation of cell volume and cellular RNA splicing processes | 3, 5 | [44] |
| NBC1 | Na+–HCO3 − cotransporter | FERM | Maintaining normal intracellular homeostasis | 5, 6 | [45] |
| PRMT3, PRMT5 | Protein arginine methyltransferase | FERM | 4.1B/DAL-1 is not itself a substrate for PRMT3/5, but rather modulates PRMT3/5-mediated methylation activity | 3, 4, 5, 6 | [44, 46] |
| β8-integrin | Cell adhesion receptor | CTD | 4.1B/DAL-1 involves in β8-integrin adhesion and signaling pathways | 6, 7 | [47, 48] |
| CD44 | Transmembrane receptor and stem cell marker | FERM | Binding of 4.1B/DAL-1 to CD44 is likely implicated in 4.1B/DAL-1 growth suppression | 8 | [14, 26] |
| PIP2 | Membrane phospholipids | FERM | PIP2 has been suggested to play a regulatory role in the association of 4.1B/DAL-1 with membrane proteins | 9 | [49] |
| TSLC-1, CADM4 | Immunoglobulin superfamily cell adhesion molecules | FERM | Organization of the actin cytoskeleton; construction of epithelial-like cell structure | 5, 6, 7 | [50, 51] |
| MPP1/2/3 | Membrane-associated guanylate kinase family members | FERM | Construction of epithelial-like cell structure | 5, 6, 7 | [52] |
| MGluR8 | Metabotropic glutamate receptors | CTD | Proper targeting and/or stabilization of mGluR8 at the plasma membrane and inhibition of mGluR8-mediated reductions in intracellular cAMP concentrations | 3, 6 | [53] |
Supported by 1 co-sedimentation assay, 2 resonant mirror detection, 3 yeast two-hybrid interaction, 4 in vitro binding assays, 5 co-immunoprecipitation, 6 GST fusion protein pull-down, 7 subcellular co-localization, 8 in vivo interaction studies, 9 PIP2-binding motifs were obtained from the UniProt database