BROWSE

Related Researcher

Author

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

ITEM VIEW & DOWNLOAD

PDZ Domain-containing 1 (PDZK1) Protein Regulates Phospholipase C-beta 3 (PLC-beta 3)-specific Activation of Somatostatin by Forming a Ternary Complex with PLC-beta 3 and Somatostatin Receptors

Cited 4 times inthomson ciCited 5 times inthomson ci
Title
PDZ Domain-containing 1 (PDZK1) Protein Regulates Phospholipase C-beta 3 (PLC-beta 3)-specific Activation of Somatostatin by Forming a Ternary Complex with PLC-beta 3 and Somatostatin Receptors
Author
Kim, Jung KukKwon, OhmanKim, JinhoKim, Eung-KyunPark, Hye KyungLee, Ji EunKim, Kyung LockChoi, Jung WoongLim, SeyoungSeok, HeonLee-Kwon, WhaseonChoi, Jang HyunKang, Byoung HeonKim, SangukRyu, Sung HoSuh, Pann-Ghill
Keywords
Complex formations; G-protein coupled receptors; Intracellular Ca; Phospholipase C; Physiological functions; Somatostatin receptors; Ternary complex
Issue Date
201206
Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Citation
JOURNAL OF BIOLOGICAL CHEMISTRY, v.287, no.25, pp.21012 - 21024
Abstract
Phospholipase C-beta(PLC-beta) is a key molecule in G protein-coupled receptor (GPCR)-mediated signaling. Many studies have shown that the four PLC-beta subtypes have different physiological functions despite their similar structures. Because the PLC-beta subtypes possess different PDZ-binding motifs, they have the potential to interact with different PDZ proteins. In this study, we identified PDZ domain-containing 1 (PDZK1) as a PDZ protein that specifically interacts with PLC-beta 3. To elucidate the functional roles of PDZK1, we next screened for potential interacting proteins of PDZK1 and identified the somatostatin receptors (SSTRs) as another protein that interacts with PDZK1. Through these interactions, PDZK1 assembles as a ternary complex with PLC-beta 3 and SSTRs. Interestingly, the expression of PDZK1 and PLC-beta 3, but not PLC-beta 1, markedly potentiated SST-induced PLC activation. However, disruption of the ternary complex inhibited SST-induced PLC activation, which suggests that PDZK1-mediated complex formation is required for the specific activation of PLC-beta 3 by SST. Consistent with this observation, the knockdown of PDZK1 or PLC-beta 3, but not that of PLC-beta 1, significantly inhibited SST-induced intracellular Ca2+ mobilization, which further attenuated subsequent ERK1/2 phosphorylation. Taken together, our results strongly suggest that the formation of a complex between SSTRs, PDZK1, and PLC-beta 3 is essential for the specific activation of PLC-beta 3 and the subsequent physiologic responses by SST.
URI
Go to Link
DOI
http://dx.doi.org/10.1074/jbc.M111.337865
ISSN
0021-9258
Appears in Collections:
SLS_Journal Papers

find_unist can give you direct access to the published full text of this article. (UNISTARs only)

Show full item record

qr_code

  • mendeley

    citeulike

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

MENU