Subtype-specific role of phospholipase C-β in bradykinin and LPA signaling through differential binding of different PDZ scaffold proteins

Choi, Jong Seob; Lim, Seyoung; Oh, Yong‐Seok; Kim, Eung Kyun; Kim, Sun Hee; Kim, Yun Hee; Heo, Kyun; JaeYoon, Kim; Kim, Jung Kuk; Yang, Yong Ryul; Ryu, Sung Ho; Suh, Pann Ghill

doi:10.1016/j.cellsig.2010.03.010

Cited by 32 publications

(33 citation statements)

References 32 publications

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“…Nevertheless, PDZK1 has been implicated in regulating a subset of GPCRs. PDZK1 promotes the formation of a complex between SSTRs and PLCb3, similar to what is observed for LPA 2 R (Oh et al, 2004;Choi et al, 2010), thereby facilitating somatostatinstimulated PLC activation, Ca 21 mobilization, and ERK1/2 phosphorylation (Kim et al, 2012). PDZK1 also functions to enhance human prostacyclin receptor (hIPR) cell surface localization and cAMP signaling and contributes to endothelial cell migration and angiogenesis (Turner et al, 2011).…”

Section: Membrane-associated Guanylate Kinase With Inverted Orientatimentioning

confidence: 84%

“…Par3 is implicated as having a role in synaptogenesis as a consequence of its interaction with BAI-1R (Duman et al, 2013). Additionally, Par3 has been shown to increase bradykinin receptor interactions with PLCb1 (Choi et al, 2010). Interestingly, both Par3 and Par6 interact and catalyze the activation of PLCb downstream of heterotrimeric G proteins and form a complex with atypical PKCs (Joberty et al, 2000; Cai et al, 2005).…”

Section: Additional Gpcr-interacting Pdz Proteinsmentioning

confidence: 99%

“…NHERF2 also interacts directly with phospholipase C (PLC) b to enhance P2Y 1 receptor-mediated Ca 21 signaling (Fam et al, 2005). Similarly, NHERF2 interacts with PLCb3 and the LPA 2 R, allowing for the formation of a protein complex that directly links the receptor to PLCb3-mediated inositol phosphate signaling (Oh et al, 2004;Choi et al, 2010). NHERF2 and mGluR5 show overlapping expression in a mouse brain at postsynaptic neuronal sites and astrocytic processes, and NHERF2 prolongs the mGluR5-mediated Ca (Fig.…”

Section: Membrane-associated Guanylate Kinase With Inverted Orientatimentioning

confidence: 99%

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PDZ Protein Regulation of G Protein–Coupled Receptor Trafficking and Signaling Pathways

Dunn

Ferguson

2015

Mol Pharmacol

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G protein-coupled receptors (GPCRs) contribute to the regulation of every aspect of human physiology and are therapeutic targets for the treatment of numerous diseases. As a consequence, understanding the myriad of mechanisms controlling GPCR signaling and trafficking is essential for the development of new pharmacological strategies for the treatment of human pathologies. Of the many GPCR-interacting proteins, postsynaptic density protein of 95 kilodaltons, disc large, zona occludens-1 (PDZ) domain-containing proteins appear most abundant and have similarly been implicated in disease mechanisms. PDZ proteins play an important role in regulating receptor and channel protein localization within synapses and tight junctions and function to scaffold intracellular signaling protein complexes. In the current study, we review the known functional interactions between PDZ domain-containing proteins and GPCRs and provide insight into the potential mechanisms of action. These PDZ domain-containing proteins include the membraneassociated guanylate-like kinases [postsynaptic density protein of 95 kilodaltons; synapse-associated protein of 97 kilodaltons; postsynaptic density protein of 93 kilodaltons; synapse-associated protein of 102 kilodaltons; discs, large homolog 5; caspase activation and recruitment domain and membrane-associated guanylate-like kinase domain-containing protein 3; membrane protein, palmitoylated 3; calcium/calmodulin-dependent serine protein kinase; membrane-associated guanylate kinase protein (MAGI)-1, MAGI-2, and MAGI-3], Na 1 /H 1 exchanger regulatory factor proteins (NHERFs) (NHERF1, NHERF2, PDZ domaincontaining kidney protein 1, and PDZ domain-containing kidney protein 2), Golgi-associated PDZ proteins (Ga-binding protein interacting protein, C-terminus and CFTR-associated ligand), PDZ domain-containing guanine nucleotide exchange factors (GEFs) 1 and 2, regulator of G protein signaling (RGS)-homology-RhoGEFs (PDZ domain-containing RhoGEF and leukemia-associated RhoGEF), RGS3 and RGS12, spinophilin and neurabin-1, SRC homology 3 domain and multiple ankyrin repeat domain (Shank) proteins (Shank1, Shank2, and Shank3), partitioning defective proteins 3 and 6, multiple PDZ protein 1, Tamalin, neuronal nitric oxide synthase, syntrophins, protein interacting with protein kinase C a 1, syntenin-1, and sorting nexin 27.

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Section: Membrane-associated Guanylate Kinase With Inverted Orientatimentioning

confidence: 84%

Section: Additional Gpcr-interacting Pdz Proteinsmentioning

confidence: 99%

Section: Membrane-associated Guanylate Kinase With Inverted Orientatimentioning

confidence: 99%

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PDZ Protein Regulation of G Protein–Coupled Receptor Trafficking and Signaling Pathways

Dunn

Ferguson

2015

Mol Pharmacol

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“…Nearly all the components of this signalling pathway are kept together by a large PDZ domaincontaining scaffold protein known as InaD, which associates with rhodopsin, TRPC, PLCb and PKC (Popescu et al, 2006;Tsunoda et al, 2001). Choi et al showed that PAR-3 mediated physical interaction between PLCb1 and the bradykinin receptor, whereas NHERF2 did so between PLCb3 and the LPA2 receptor (Choi et al, 2010). The association of NHERF1 and/or NHERF2 with the parathyroid hormone 1 receptor (PTH1R) (Mahon and Segre, 2004;Sneddon et al, 2003;Wang et al, 2009;Wheeler et al, 2008), purinergic receptor (P2RY1) (Fam et al, 2005) and metabotropic glutamate receptor 5 (mGluR5) (Paquet et al, 2006), can enhance their PLCb-mediated signalling (Ritter and Hall, 2009).…”

Section: Discussionmentioning

confidence: 99%

WDR36 acts as a scaffold protein tethering a G-protein-coupled receptor, Gαq and phospholipase Cβ in a signalling complex

Cartier

Parent

Labrecque

et al. 2011

Journal of Cell Science

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SummaryWe identified the WD-repeat-containing protein, WDR36, as an interacting partner of the b isoform of thromboxane A 2 receptor (TPb) by yeast two-hybrid screening. We demonstrated that WDR36 directly interacts with the C-terminus and the first intracellular loop of TPb by in vitro GST-pulldown assays. The interaction in a cellular context was observed by co-immunoprecipitation, which was positively affected by TPb stimulation. TPb-WDR36 colocalization was detected by confocal microscopy at the plasma membrane in non-stimulated HEK293 cells but the complex translocated to intracellular vesicles following receptor stimulation. Coexpression of WDR36 and its siRNA-mediated knockdown, respectively, increased and inhibited TPb-induced Gaq signalling. Interestingly, WDR36 co-immunoprecipitated with Gaq, and promoted TPb-Gaq interaction. WDR36 also associated with phospholipase Cb (PLCb) and increased the interaction between Gaq and PLCb, but prevented sequestration of activated Gaq by GRK2. In addition, the presence of TPb in PLCb immunoprecipitates was augmented by expression of WDR36. Finally, disease-associated variants of WDR36 affected its ability to modulate Gaq-mediated signalling by TPb. We report that WDR36 acts as a new scaffold protein tethering a G-proteincoupled receptor, Gaq and PLCb in a signalling complex.

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“…All PLC-␤ isoforms contain consensus PDZ motifs, -X(S/T)X(L/V)-COOH (X represents any amino acid), at their carboxyl termini (21). The C terminus of PLC-␤3, but not other PLC-␤ isoforms, was reported to specifically interact with the PDZ domains of NHERF2 in mouse small intestine (19), and Shank2, a PDZ protein present in the postsynaptic density in neuronal cells (22), whereas the PLC-␤1 C-tail reportedly interacts with PAR-3, a PDZ scaffold protein in HeLa cells (23). Most recently, it was reported that in NHERF1 knock-out mice, PLC-␤3 was down-regulated in mouse jejuna villus cells (24).…”

mentioning

confidence: 99%

A Chemokine Receptor CXCR2 Macromolecular Complex Regulates Neutrophil Functions in Inflammatory Diseases

Wang

Farooq

et al. 2012

Journal of Biological Chemistry

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Subtype-specific role of phospholipase C-β in bradykinin and LPA signaling through differential binding of different PDZ scaffold proteins

Cited by 32 publications

References 32 publications

PDZ Protein Regulation of G Protein–Coupled Receptor Trafficking and Signaling Pathways

PDZ Protein Regulation of G Protein–Coupled Receptor Trafficking and Signaling Pathways

WDR36 acts as a scaffold protein tethering a G-protein-coupled receptor, Gαq and phospholipase Cβ in a signalling complex

A Chemokine Receptor CXCR2 Macromolecular Complex Regulates Neutrophil Functions in Inflammatory Diseases

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