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Start Over Author "Han, Seung Jin" Journal biochemical and biophysical research communications
7 results on '"Han, Seung Jin"'

7. AP180 binds to the C-terminal SH2 domain of phospholipase C-gamma1 and inhibits its enzymatic activity.

Author

Han SJ, Lee JH, Hong SH, Park SD, Kim CG, Song MD, Park TK, and Kim CG

Subjects
Adaptor Proteins, Vesicular Transport, Amino Acid Sequence, Animals, Blotting, Western, Brain enzymology, Brain metabolism, Clathrin metabolism, Endocytosis, Enzyme Inhibitors pharmacology, Glutathione Transferase metabolism, Immunoblotting, Isoenzymes antagonists & inhibitors, Isoenzymes physiology, Molecular Sequence Data, Peptides chemistry, Phospholipase C gamma, Precipitin Tests, Protein Binding, Protein Structure, Tertiary, Rats, Recombinant Fusion Proteins metabolism, Signal Transduction, Subcellular Fractions, Time Factors, Type C Phospholipases antagonists & inhibitors, Type C Phospholipases physiology, src Homology Domains, Carrier Proteins chemistry, Carrier Proteins metabolism, Isoenzymes metabolism, Membrane Proteins chemistry, Membrane Proteins metabolism, Monomeric Clathrin Assembly Proteins, Type C Phospholipases metabolism
Abstract

The role of phospholipase Cgamma1 (PLCgamma1) in signal transduction was investigated by characterizing its SH domain-binding proteins that may represent components of a novel signaling pathway. A 180-kDa protein that binds to the SH2 domain of PLCgamma1 was purified from rat brain. The amino acid sequence of peptide derived from the purified protein is now identified as AP180, a clathrin assembly protein that has been implicated in clathrin-mediated synaptic vesicle recycling in synapses. In this report, we demonstrate the stable association of PLCgamma1 with AP180 in a clathrin-coated vesicle complex, which not only binds to the carboxyl-terminal SH2 domain of PLCgamma1, but also inhibits its enzymatic activity in a dose-dependent manner., ((c)2002 Elsevier Science.)

Published
2002
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