The C2 domains of classical/conventional PKCs are specific PtdIns(4,5)P(2)-sensing domains
| Autor: | Juan C. Gómez-Fernández, Senena Corbalán-García, Marta Guerrero-Valero, Consuelo Marín-Vicente |
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| Rok vydání: | 2007 |
| Předmět: |
chemistry.chemical_classification
Models Molecular Phosphatidylinositol 4 5-Diphosphate Effector Protein Conformation PKCS Phosphatidylserine Biology Biochemistry Cell biology chemistry.chemical_compound Membrane docking Enzyme Membrane chemistry Protein kinase A Protein Kinase C C2 domain Protein Binding |
| Zdroj: | Biochemical Society transactions. 35(Pt 5) |
| ISSN: | 0300-5127 |
| Popis: | The C2 domains of cPKCs [classical/conventional PKCs (protein kinase Cs)] bind to membranes in a Ca 2+ -dependent manner and thereby act as cellular Ca 2+ effectors. Recent findings have demonstrated that the C2 domain of cPKCs interacts specifically with PtdIns(4,5) P 2 through its polybasic cluster located in the β3–β4-strands, this interaction being critical for the membrane localization of these enzymes in living cells. In addition, these C2 domains exhibit higher affinity to bind PtdIns(4,5) P 2 than any other polyphosphate phosphatidylinositols. It has also been shown that the presence of PtdIns(4,5) P 2 in model membranes decreases the Ca 2+ concentration required for classical C2 domains to bind them. Overall, the studies reviewed here suggest a new mechanism of membrane docking by the C2 domains of cPKCs in which the local densities of phosphatidylserine and PtdIns(4,5) P 2 on the inner leaflet of the plasma membrane are sufficient to drive Ca 2+ -activated membrane docking during a physiological Ca 2+ signal. |
| Databáze: | OpenAIRE |
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