Myristoylated and non-myristoylated forms of the pH sensor protein hisactophilin II: intracellular shuttling to plasma membrane and nucleus monitored in real time by a fusion with green fluorescent protein
| Autor: | Renate Albrecht, Christoph Eckerskorn, Monika Matzner, G. Gerisch, Frank Hanakam |
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| Rok vydání: | 1996 |
| Předmět: |
Time Factors
Green Fluorescent Proteins Molecular Sequence Data Protozoan Proteins Plasma protein binding Biology Myristic Acid General Biochemistry Genetics and Molecular Biology Green fluorescent protein Fungal Proteins Cell membrane medicine Animals Dictyostelium Amino Acid Sequence Molecular Biology Histidine Myristoylation Cell Nucleus Fungal protein General Immunology and Microbiology General Neuroscience Cell Membrane Microfilament Proteins Biological Transport Hydrogen-Ion Concentration Fusion protein Actins Cell biology Luminescent Proteins medicine.anatomical_structure Cytoplasm Carrier Proteins Myristic Acids Research Article Protein Binding |
| Zdroj: | The EMBO Journal. 15:2935-2943 |
| ISSN: | 0261-4189 |
| DOI: | 10.1002/j.1460-2075.1996.tb00656.x |
| Popis: | Hisactophilins are myristoylated proteins that are rich in histidine residues and known to exist in Dictyostelium cells in a plasma membrane-bound and a soluble cytoplasmic state. Intracellular translocation of these proteins in response to pH changes was monitored using hisactophilin fusions with green fluorescent protein (GFP) and confocal laser scanning microscopy. Both the normal and a mutated non-myristoylated fusion protein shuffled within the cells in a pH-dependent manner. After lowering the pH, these proteins translocated within minutes between the cytoplasm, the plasma membrane and the nucleus. The role of histidine clusters on the surface of hisactophilin molecules in binding of the proteins to the plasma membrane and in their transfer to the nucleus is discussed on the basis of a pH switch mechanism. |
| Databáze: | OpenAIRE |
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