Phospholipase Cepsilon guanine nucleotide exchange factor activity and activation of Rap1.
Phospholipase C (PLC) epsilon is directly regulated by Ras and Rap1 small GTPases: Ras and Rap1, in their GTP-bound form, interact with the Ras/Rap1-associationg (RA) domain of PLCepsilon, thereby translocating PLCepsilon to the plasma membrane and the Golgi apparatus, respectively. In the plasma membrane and the Golgi apparatus, PLCepsilon acts as a phosphoinositide-specific PLC, regulating various downstream signaling pathways. PLCepsilon also contains a CDC25 homology domain, which enhances guanine nucleotide exchange on Rap1. Here, we describe biochemical characterization of the CDC25 homology domain of PLCepsilon and provide insights into its physiological role in the regulation of PLCepsilon activity.
Satoh
Takaya
T
Division of Molecular Biology, Department of Molecular and Cellular Biology, Kobe University, Graduate School of Medicine, Kobe, Japan.
Edamatsu
Hironori
H
Kataoka
Tohru
T
D000818:Animals; D019556:COS Cells; D002522:Chlorocebus aethiops; D006160:Guanosine Triphosphate / Q000378:metabolism; D015544:Inositol 1,4,5-Trisphosphate / Q000378:metabolism; D054801:Phosphoinositide Phospholipase C / Q000378:metabolism*; D021381:Protein Transport; D018411:Spodoptera; D020827:rap1 GTP-Binding Proteins / Q000378:metabolism*; D020666:ras-GRF1 / Q000378:metabolism*
D020666:ras-GRF1; D015544:Inositol 1,4,5-Trisphosphate; D006160:Guanosine Triphosphate; D054801:Phosphoinositide Phospholipase C; C423320:phospholipase C epsilon; D020827:rap1 GTP-Binding Proteins