Interaction of Phospholipase C γ 1 via Its COOH-Terminal SRC Homology 2 Domain with Synaptojanin
| Autor: | Joon-Ki Chung, Tae Kyu Park, Chan Gil Kim, Soo Jung Ahn, Hyo Jung Mo, Seung Hwan Hong, Seung-Jin Han |
|---|---|
| Rok vydání: | 1998 |
| Předmět: |
Recombinant Fusion Proteins
Biophysics Nerve Tissue Proteins Peptide Synaptojanin Biology SH2 domain Biochemistry Synaptic vesicle Substrate Specificity src Homology Domains Animals Receptors Platelet-Derived Growth Factor Amino Acid Sequence Molecular Biology chemistry.chemical_classification Epidermal Growth Factor Phospholipase C Phospholipase C gamma Binding protein Brain Receptor Protein-Tyrosine Kinases Cell Biology Phosphoric Monoester Hydrolases Rats Cell biology Enzyme Activation Isoenzymes Molecular Weight chemistry Type C Phospholipases Signal transduction Protein Binding Proto-oncogene tyrosine-protein kinase Src |
| Zdroj: | Biochemical and Biophysical Research Communications. 244:62-67 |
| ISSN: | 0006-291X |
| DOI: | 10.1006/bbrc.1998.8220 |
| Popis: | The role of the phospholipase C gamma 1 (PLC gamma 1) in signal transduction was investigated by characterizing its interactions with proteins that may represent components of a novel signalling pathway. A 145-kDa protein that binds SH2 domain of PLC gamma 1 was purified from rat brain. The sequence of peptide derived from the purified binding protein now identify it as synaptojanin, a nerve terminal protein that has been implicated in the endocytosis of fused synaptic vesicles and shown to be a member of the inositol polyphosphate 5-phosphatase family. We demonstrate here stable association of PLC gamma 1 with synaptojanin, a protein that not only binds carboxyl terminal SH2 domain of PLC gamma 1, but also inhibits PLC gamma 1 activity. |
| Databáze: | OpenAIRE |
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