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

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Regulation of phospholipase C-beta 3 activity by Na+/H+ exchanger regulatory factor 2

Cited 74 times inthomson ciCited 75 times inthomson ci
Title
Regulation of phospholipase C-beta 3 activity by Na+/H+ exchanger regulatory factor 2
Author
Hwang, JIHeo, KShin, KJKim, EYun, CHCRyu, SHShin, HSSuh, Pann-Ghill
Issue Date
2000-06
Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Citation
JOURNAL OF BIOLOGICAL CHEMISTRY, v.275, no.22, pp.16632 - 16637
Abstract
Among the phospholipase C that catalyzes the hydrolysis of phosphatidylinositol 4,5-bisphosphate, four mammalian phospholipase C-beta (PLC-beta) isotypes (isotypes 1-4) are activated through G protein-coupled receptors (GPCRs). Although the regulation of the PLC-beta s by GPCRs and heterotrimeric G proteins has been extensively studied, little is known about the molecular determinants that regulate their activity. The PLC-beta isozymes carry a putative PSD-95/Dlg/ZO-1 (PDZ) binding motif (X(S/T)X(V/L)COOH) at their carboxyl terminus, which is implicated in specific interactions with anchor proteins. Using the yeast two-hybrid system, me identified Na+/H+ exchanger regulatory factor 2 (NHERF2) as a protein that interacted with a C-terminal heptapeptide of PLC-beta 3. Immunoprecipitation studies revealed that NHERF2 interacts specifically with PLC-beta 3, but not with other PLC-beta isotypes. Furthermore, PLC-beta 3 interacted with NHERF2 rather than with other PDZ-containing proteins. This interaction required the COOH-terminal NTQL sequence of PLC-beta 3 and the second PDZ domain of NHERF2. Interestingly, NHERF2 potentiated the PLC-beta activation by carbachol in COS7 and HeLa cells, while mutant NHERF2, lacking the second PDZ domain, had no such effect. Taken together, the data suggest that NHERF2 may act as a modulator underlying the process of PLC-beta 3-mediated signaling
URI
https://scholarworks.unist.ac.kr/handle/201301/16452
DOI
10.1074/jbc.M001410200
ISSN
0021-9258
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