A comparative analysis of the phosphoinositide binding specificity of pleckstrin homology domains
| Autor: | Lucia E. Rameh, Michael P. Czech, Steven J. Burakoff, Anthony D. Couvillon, Kodimangalam S. Ravichandran, Lewis C. Cantley, Da Sheng Wang, Barbara VanRenterghem, Ann Kristin Arvidsson, Gary Rathbun, Ching Shih Chen, Anne M. Crompton, Kermit L. Carraway |
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| Rok vydání: | 1997 |
| Předmět: |
Phosphotyrosine binding
Phosphatidylinositol 4 5-Diphosphate Receptors Steroid Molecular Sequence Data Plasma protein binding Biology Biochemistry Phosphatidylinositol Phosphates Agammaglobulinaemia Tyrosine Kinase Animals Amino Acid Sequence Binding site Phosphotyrosine Molecular Biology Binding Sites Signal transducing adaptor protein Membrane Proteins Proteins Spectrin Cell Biology Blood Proteins Protein-Tyrosine Kinases Phosphoproteins IRS1 Cell biology Pleckstrin homology domain Kinetics Son of Sevenless Proteins Phosphotyrosine-binding domain Binding domain Protein Binding |
| Zdroj: | The Journal of biological chemistry. 272(35) |
| ISSN: | 0021-9258 |
| Popis: | Pleckstrin homology (PH) and phosphotyrosine binding (PTB) domains are structurally related regulatory modules that are present in a variety of proteins involved in signal transduction, such as kinases, phospholipases, GTP exchange proteins, and adapter proteins. Initially these domains were shown to mediate protein-protein interactions, but more recently they were also found to bind phosphoinositides. Most studies to date have focused on binding of PH domains to phosphatidylinositol (PtdIns)-4-P and PtdIns-4,5-P2 and have not considered the lipid products of phosphoinositide 3-kinase: PtdIns-3-P, PtdIns-3,4-P2, and PtdIns-3,4,5-P3. Here we have compared the phosphoinositide specificity of six different PH domains and the Shc PTB domain using all five phosphoinositides. We show that the Bruton's tyrosine kinase PH domain binds to PtdIns-3,4, 5-P3 with higher affinity than to PtdIns-4,5-P2, PtdIns-3,4-P2 or inositol 1,3,4,5-tetrakisphosphate (Ins-1,3,4,5-P4). This selectivity is decreased by the xid mutation (R28C). Selective binding of PtdIns-3,4,5-P3 over PtdIns-4,5-P2 or PtdIns-3,4-P2 was also observed for the amino-terminal PH domain of T lymphoma invasion and metastasis protein (Tiam-1), the PH domains of Son-of-sevenless (Sos) and, to a lesser extent, the PH domain of the beta-adrenergic receptor kinase. The oxysterol binding protein and beta-spectrin PH domains bound PtdIns-3,4,5-P3 and PtdIns-4,5-P2 with similar affinities. PtdIns-3,4,5-P3 and PtdIns-4,5-P2 also bound to the PTB domain of Shc with similar affinities and lipid binding was competed with phosphotyrosine (Tyr(P)-containing peptides. These results indicate that distinct PH domains select for different phosphoinositides. |
| Databáze: | OpenAIRE |
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