PDZ domain-containing 1 (PDZK1) protein regulates phospholipase C-β3 (PLC-β3)-specific activation of somatostatin by forming a ternary complex with PLC-β3 and somatostatin receptors (Q36033180)

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English	PDZ domain-containing 1 (PDZK1) protein regulates phospholipase C-β3 (PLC-β3)-specific activation of somatostatin by forming a ternary complex with PLC-β3 and somatostatin receptors	scientific article

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scholarly article

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11 August 2017

PDZ domain-containing 1 (PDZK1) protein regulates phospholipase C-β3 (PLC-β3)-specific activation of somatostatin by forming a ternary complex with PLC-β3 and somatostatin receptors (English)

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11 August 2017

Byoung Heon Kang

13

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Byoung Heon Kang

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11 August 2017

16

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Pann-Ghill Suh

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11 August 2017

author name string

Jung Kuk Kim

1

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11 August 2017

Ohman Kwon

2

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11 August 2017

Jinho Kim

3

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11 August 2017

Eung-Kyun Kim

4

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11 August 2017

Hye Kyung Park

5

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11 August 2017

Ji Eun Lee

6

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11 August 2017

Kyung Lock Kim

7

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11 August 2017

Jung Woong Choi

8

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11 August 2017

Seyoung Lim

9

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11 August 2017

Heon Seok

10

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11 August 2017

Whaseon Lee-Kwon

11

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11 August 2017

Jang Hyun Choi

12

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11 August 2017

Sanguk Kim

14

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11 August 2017

Sung Ho Ryu

15

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11 August 2017

language of work or name

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publication date

23 April 2012

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11 August 2017

Journal of Biological Chemistry

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11 August 2017

287

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11 August 2017

25

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11 August 2017

21012-21024

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Europe PubMed Central

PMC publication ID

11 August 2017

Rewiring of PDZ domain-ligand interaction network contributed to eukaryotic evolution

1 reference

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2 October 2017

Phospholipase C-η1 is activated by intracellular Ca(2+) mobilization and enhances GPCRs/PLC/Ca(2+) signaling

1 reference

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Subtype-specific roles of phospholipase C-β via differential interactions with PDZ domain proteins.

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Proteome scanning to predict PDZ domain interactions using support vector machines

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PDZ domains and their binding partners: structure, specificity, and modification

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2 October 2017

Quantifying protein-protein interactions in high throughput using protein domain microarrays

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Role of the adaptor protein PDZK1 in controlling the HDL receptor SR-BI

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Short Linear Motifs recognized by SH2, SH3 and Ser/Thr Kinase domains are conserved in disordered protein regions

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Multiple roles of phosphoinositide-specific phospholipase C isozymes

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Genome-wide prediction of SH2 domain targets using structural information and the FoldX algorithm.

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Intrinsic disorder in the C-terminal domain of the Shaker voltage-activated K+ channel modulates its interaction with scaffold proteins

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2 October 2017

PDZ domain binding selectivity is optimized across the mouse proteome

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Local structural disorder imparts plasticity on linear motifs.

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What are DNA sequence motifs?

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Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling

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Interactions with PDZ domain proteins PIST/GOPC and PDZK1 regulate intracellular sorting of the somatostatin receptor subtype 5.

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The interaction of phospholipase C-beta3 with Shank2 regulates mGluR-mediated calcium signal

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PDZBase: a protein-protein interaction database for PDZ-domains

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NHERF2 specifically interacts with LPA2 receptor and defines the specificity and efficiency of receptor-mediated phospholipase C-beta3 activation

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Stimulation by parathyroid hormone of a NHERF-1-assembled complex consisting of the parathyroid hormone I receptor, phospholipase Cbeta, and actin increases intracellular calcium in opossum kidney cells

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Opportunities in somatostatin research: biological, chemical and therapeutic aspects

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Signal transduction of somatostatin in human B lymphoblasts

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Distinct binding specificity of the multiple PDZ domains of INADL, a human protein with homology to INAD from Drosophila melanogaster

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Regulation of phosphoinositide-specific phospholipase C

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PDZK1 and GREB1 are estrogen-regulated genes expressed in hormone-responsive breast cancer.

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Identification of a PDZ-domain-containing protein that interacts with the scavenger receptor class B type I

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

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Two distantly positioned PDZ domains mediate multivalent INAD-phospholipase C interactions essential for G protein-coupled signaling

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Phospholipase C activation and Ca2+ mobilization by cloned human somatostatin receptor subtypes 1-5, in transfected COS-7 cells

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Somatostatin receptors 1, 2, and 5 cooperate in the somatostatin inhibition of C6 glioma cell proliferation in vitro via a phosphotyrosine phosphatase-eta-dependent inhibition of extracellularly regulated kinase-1/2.

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12 December 2020

based on heuristic

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P2Y2 purinergic and M3 muscarinic acetylcholine receptors activate different phospholipase C-beta isoforms that are uniquely susceptible to protein kinase C-dependent phosphorylation and inactivation

1 reference

https://pubmed.ncbi.nlm.nih.gov/22528496

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

PDZ-domain arrays for identifying components of GPCR signaling complexes

1 reference

https://pubmed.ncbi.nlm.nih.gov/22528496

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based on heuristic

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All five cloned human somatostatin receptors (hSSTR1-5) are functionally coupled to adenylyl cyclase

1 reference

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Identifiers

10.1074/JBC.M111.337865

1 reference

Europe PubMed Central

PMC publication ID

11 August 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

11 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

11 August 2017

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