Pleckstrin homology domain of phospholipase C-gamma1 directly binds to 68-kDa neurofilament light chain
Experimental & Molecular Medicine
;
: 265-272, 2006.
Artículo
en Inglés
| WPRIM
| ID: wpr-96564
ABSTRACT
Phosphoinositide-specific phospholipase C-gamma1 (PLC-gamma1) 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-gamma1 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-gamma1. NF-L is known as a component of neuronal intermediate filaments, which are responsible for supporting the structure of myelinated axons in neuron. PLC-gamma1 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-gamma1 was slightly decreased in the presence of purified NF-L in vitro, suggesting that NF-L inhibits PLC-gamma1. Our results suggest that PLC-gamma1-associated NF-L sequesters the phospholipid from the PH domain of PLC-gamma1.
Texto completo:
Disponible
Índice:
WPRIM (Pacífico Occidental)
Asunto principal:
Péptidos
/
Fosfoproteínas
/
Unión Proteica
/
Biosíntesis de Proteínas
/
Sitios de Unión
/
Datos de Secuencia Molecular
/
Proteínas Sanguíneas
/
Secuencia de Aminoácidos
/
Células PC12
/
Proteínas de Neurofilamentos
Tipo de estudio:
Estudio pronóstico
Límite:
Animales
Idioma:
Inglés
Revista:
Experimental & Molecular Medicine
Año:
2006
Tipo del documento:
Artículo
Similares
MEDLINE
...
LILACS
LIS