Differential expression of regulator of G‐protein signaling R12 subfamily members during mouse development

Martin-McCaffrey, Luke; Hains, Melinda D.; Pritchard, Grant A.; Pająk, Agnieszka; Dagnino, Lina; Siderovski, David P.; D’Souza, Sudhir J.A.

doi:10.1002/dvdy.20555

Cited by 13 publications

(19 citation statements)

References 27 publications

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“…Studies in COS-7 and HEK293 cells, have reported that endogenous or ectopically expressed RGS12 segregates into nuclear locations, thus suggesting its involvement in the regulation of transcription and cell cycle (Chatterjee and Fisher, 2000b;. However, more recent studies in mouse embryos from E7.5 onward revealed that, in vivo, RGS12 is mostly localized in the cytoplasm at any stage of mouse embryogenesis in the tissues examined, thus suggesting that nuclear localization of RGS12 may vary depending on the cell type or, alternatively, indicating that immortalized/transformed cell lines may possess subcellular RGS12 protein distributions different to cells in native tissues (Martin-McCaffrey et al, 2005a).…”

Section: Rgs12mentioning

confidence: 91%

“…RGS14 is widely expressed in mammal tissues (Buckbinder et al, 1997;Evans et al, 2014;Jia et al, 2012;Lim et al, 2013;Martin-McCaffrey et al, 2005a;Oner et al, 2013;Vellano et al, 2013;Yasui et al, 2013;Zhao et al, 2013), such as brain (Lopez-Aranda et al, 2006;Snow et al, 1997), lymphoid organs (Larminie et al, 2004;Snow et al, 1997) and lung , and cells, such as lymphocytes (Larminie et al, 2004), in pyramidal and nonpyramidal cell types in brain cortex in astrocytes (Lopez-Aranda et al, 2006) and in low rate in platelets (Kim et al, 2006).…”

Section: Rgs14 (A28-rgs14)mentioning

confidence: 96%

“…RGS12 has also been reported to be mostly expressed in trigeminal and dorsal root ganglia (DRG) neurons and muscle in the E14.5 embryonic mouse suggesting a role for mammalian RGS12 in myo-and neurogenesis (Martin-McCaffrey et al, 2005a), and also in the thalamus of adult monkey (Lopez-Aranda et al, 2006). Studies in COS-7 and HEK293 cells, have reported that endogenous or ectopically expressed RGS12 segregates into nuclear locations, thus suggesting its involvement in the regulation of transcription and cell cycle (Chatterjee and Fisher, 2000b;.…”

Section: Rgs12mentioning

confidence: 96%

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Regulators of G-Protein-Signaling Proteins: Negative Modulators of G-Protein-Coupled Receptor Signaling

Woodard

Jardín

Berna‐Erro

et al. 2015

International Review of Cell and Molecular Biology

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Section: Rgs12mentioning

confidence: 91%

Section: Rgs14 (A28-rgs14)mentioning

confidence: 96%

Section: Rgs12mentioning

confidence: 96%

See 1 more Smart Citation

Regulators of G-Protein-Signaling Proteins: Negative Modulators of G-Protein-Coupled Receptor Signaling

Woodard

Jardín

Berna‐Erro

et al. 2015

International Review of Cell and Molecular Biology

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“…They contain additional functional domains such as a PDZ binding motif, a GoLoco motif and Rap binding domain at the very C‐terminal end of the proteins. At the amino‐terminus, these proteins present a PDZ domain and a phosphotyrosine‐binding (PTB) domain, both of which promote protein–protein interactions (Ross and Wilkie, 2000; Martin‐McCaffrey et al ., 2005). The PTB domain can associate with tyrosine‐phosphorylated N‐type calcium channels, therefore regulating calcium signalling (Schiff et al ., 2000; Richman et al ., 2005).…”

Section: Regulators Of G‐protein Signalling (Rgs)mentioning

confidence: 99%

Regulation of GPCR activity, trafficking and localization by GPCR‐interacting proteins

Magalhães

Dunn

Ferguson

2012

British J Pharmacology

308

290

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GPCRs represent the largest family of integral membrane proteins and were first identified as receptor proteins that couple via heterotrimeric G-proteins to regulate a vast variety of effector proteins to modulate cellular function. It is now recognized that GPCRs interact with a myriad of proteins that not only function to attenuate their signalling but also function to couple these receptors to heterotrimeric G-protein-independent signalling pathways. In addition, intracellular and transmembrane proteins associate with GPCRs and regulate their processing in the endoplasmic reticulum, trafficking to the cell surface, compartmentalization to plasma membrane microdomains, endocytosis and trafficking between intracellular membrane compartments. The present review will overview the functional consequence of b-arrestin, receptor activity-modifying proteins (RAMPS), regulators of G-protein signalling (RGS), GPCR-associated sorting proteins (GASPs), Homer, small GTPases, PSD95/Disc Large/Zona Occludens (PDZ), spinophilin, protein phosphatases, calmodulin, optineurin and Src homology 3 (SH3) containing protein interactions with GPCRs. LINKED ARTICLESThis article is part of a themed section on the Molecular Pharmacology of G Protein-Coupled Receptors (GPCRs). To view the other articles in this section visit http://dx.doi.org/10.1111/bph.2012.165.issue-6. To view the 2010 themed section on the same topic visit http://onlinelibrary.wiley.com/doi/10.1111/bph.2010.159.issue-5/issuetoc Abbreviations 5-HT2AR, serotonin receptor subtype 2; 5HT2CR, serotonin 2C receptor; a1DAR, a1D adrenergic receptor; Arf6, ADP-ribosylation factor 6; ARNO, ARF nucleotide-binding site opener; AT1R, angiotensin II type 1 receptor; b2AR, b2-adrenergic receptor; CAL, cystic fibrosis transmembrane conductance regulator-associated ligand; CASK, calcium/calmodulin-dependent serine protein kinase; CaSR, calcium sensing receptor; cGRP1/cGRP2, calcitonin gene-related peptides; CIPP, channel-interacting PDZ protein; CRF, corticotrophin-releasing factor; CRFR1, corticotropin releasing factor receptor 1; CRLR, calcitonin-like receptor; CXCR2, IL-8 receptor B; CXCR4, chemokine receptor type 4; EBP50, ERM-binding phosphoprotein 50; EEA1, effector early endosome antigen 1; EVH, ENA/VASP homology domain; GABAB, GABA type B receptor; GAPs, GTPase activating proteins; GASP, GPCR-associated sorting protein; GDP, guanosine diphosphate; GEFs, guanine nucleotide exchange factors; GIPC, GIPC PDZ domain containing family member 1; GRB2, growth factor receptor-bound protein 2; GRKs, GPCR kinases; MAGI, membrane-associated guanylate kinase inverted; MAGUK, membrane-associated guanylate kinase; mGluRs, metabotropic glutamate receptors; MINT1, Munc-18-interacting protein 1; MPP3, p55 subfamily member 3; MT1, melatonin type 1 receptor; MUPP1, multi-PDZ-domain protein; Nck, non-catalytic region of tyrosine kinase adaptor protein; NHERF, Na + /H + exchanger regulatory factor 1; NSF, N-ethylmaleimide-sensitive factor; P2Y1, P2Y1 purinergic receptors; PAK, p21-activated kinase...

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“…RGS12 mRNA is expressed in rat spleen, lung, prostate, testis, ovary, kidney and brain (117). The expression of RGS12 is also detected at different embryonic stages during mouse development (118). Due to its multi-domain architecture, RGS12 protein has the potential to regulate multiple signaling pathway components.…”

Section: Regulation Of Differentiation and Function Of Bone Cell Bmentioning

confidence: 99%

Role of regulator of G protein signaling proteins in bone

et al. 2014

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Regulators of G protein signaling (RGS) proteins are a family with more than 30 proteins that all contain an RGS domain. In the past decade, increasing evidence has indicated that RGS proteins play crucial roles in the regulation of G protein coupling receptors (GPCR), G proteins, and calcium signaling during cell proliferation, migration, and differentiation in a variety of tissues. In bone, those proteins modulate bone development and remodeling by influencing various signaling pathways such as GPCR-G protein signaling, Wnt, calcium oscillations and PTH. This review summarizes the recent advances in the understanding of the regulation of RGS genes expression, as well as the functions and mechanisms of RGS proteins, especially in regulating GPCR-G protein signaling, Wnt signaling, calcium oscillations signaling and PTH signaling during bone development and remodeling. This review also highlights the regulation of different RGS proteins in osteoblasts, chondrocytes and osteoclasts. The knowledge from the recent advances of RGS study summarized in the review would provide the insights into new therapies for bone diseases.

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Differential expression of regulator of G‐protein signaling R12 subfamily members during mouse development

Abstract: Regulators of G-protein Signaling (RGS proteins)

Cited by 13 publications

References 27 publications

Regulators of G-Protein-Signaling Proteins: Negative Modulators of G-Protein-Coupled Receptor Signaling

Regulators of G-Protein-Signaling Proteins: Negative Modulators of G-Protein-Coupled Receptor Signaling

Regulation of GPCR activity, trafficking and localization by GPCR‐interacting proteins

Role of regulator of G protein signaling proteins in bone

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