Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Brain / enzymology
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Enzyme Activation / drug effects
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Enzyme Activation / genetics
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Epidermal Growth Factor / metabolism
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Isoenzymes / antagonists & inhibitors
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Isoenzymes / physiology*
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Molecular Weight
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Nerve Tissue Proteins / physiology*
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Phospholipase C gamma
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Phosphoric Monoester Hydrolases / physiology*
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Protein Binding / genetics
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Rats
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Receptor Protein-Tyrosine Kinases / metabolism
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Receptors, Platelet-Derived Growth Factor / metabolism
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Recombinant Fusion Proteins / metabolism
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Substrate Specificity
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Type C Phospholipases / antagonists & inhibitors
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Type C Phospholipases / physiology*
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src Homology Domains / genetics
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src Homology Domains / physiology*
Substances
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Isoenzymes
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Nerve Tissue Proteins
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Recombinant Fusion Proteins
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Epidermal Growth Factor
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Receptor Protein-Tyrosine Kinases
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Receptors, Platelet-Derived Growth Factor
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synaptojanin
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Phosphoric Monoester Hydrolases
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Type C Phospholipases
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Phospholipase C gamma