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Suh, Pann-Ghill
BioSignal Network Lab (BSN)
Research Interests
  • Signal transduction, cancer, metabolism, phospholipase C

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Pleckstrin homology domain of phospholipase C-gamma 1 directly binds to 68-kDa neurofilament light chain

Cited 9 times inthomson ciCited 10 times inthomson ci
Title
Pleckstrin homology domain of phospholipase C-gamma 1 directly binds to 68-kDa neurofilament light chain
Author
Kim, Sung-KukChoi, Jang HyunSuh, Pann-GhillChang, Jong-Soo
Keywords
Neurofilament protein L; PC12 cells; Phosphatidylinositol 4,5-diphosphate; Phospholipase C gamma; Protein interaction mapping
Issue Date
200606
Publisher
KOREAN SOC MED BIOCHEMISTRY MOLECULAR BIOLOGY
Citation
EXPERIMENTAL AND MOLECULAR MEDICINE, v.38, no.3, pp.265 - 272
Abstract
Phosphoinositide-specific phospholipase C-γ1 (PLC-γ1) has two pleckstrin homology (PH) domains: an amino-terminal domain (PH1) and a split PH domain (PH2). Here, we show that overlay assay of bovine brain tubulin pool with glutathione-S-transferase (GST)-PLC-γ1 PH domain fusion proteins, followed by matrix-assisted laser-desorption ionization-time of flight mass spectrometry (MALDI-TOF MS), identified 68-kDa neurofilament light chain (NF-L) as a binding protein of amino-terminal PH domain of PLC-γ1. NF-L is known as a component of neuronal intermediate filaments, which are responsible for supporting the structure of myelinated axons in neuron. PLC-γ1 and NF-L colocalized in the neurite in PC12 cells upon nerve growth factor stimulation. In vitro binding assay and immunoprecipitation analysis also showed a specific interaction of both proteins in differentiated PC12 cells. The phosphatidylinositol 4, 5-bisphosphate [PI(4,5)P2] hydrolyzing activity of PLC-γ1 was slightly decreased in the presence of purified NF-L in vitro, suggesting that NF-L inhibits PLC-γ1. Our results suggest that PLC-γ1-associated NF-L sequesters the phospholipid from the PH domain of PLC-γ1.
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ISSN
1226-3613
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