RGS14: Difference between revisions

Jump to navigation Jump to search
m (Robot: Automated text replacement (-{{reflist}} +{{reflist|2}}, -<references /> +{{reflist|2}}, -{{WikiDoc Cardiology Network Infobox}} +))
 
imported>JCW-CleanerBot
m (→‎Further reading: task, replaced: Cellular Signalling. → Cellular Signalling (2))
 
(One intermediate revision by one other user not shown)
Line 1: Line 1:
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Regulator of G-protein signaling 14''' (RGS14) is a [[protein]] that in humans is encoded by the ''RGS14'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RGS14 regulator of G-protein signalling 14| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10636| accessdate = }}</ref>
| update_page = yes
 
| require_manual_inspection = no
== Function ==
| update_protein_box = yes
 
| update_summary = yes
RGS14 is a member of the [[regulator of G protein signalling]] family. This protein contains one [[RGS domain]], two [[Raf-like Ras-binding domain]]s (RBDs), and one [[GoLoco motif]]. The protein attenuates the signaling activity of [[G-protein]]s by binding, through its GoLoco domain, to specific types of activated, [[guanosine triphosphate|GTP]]-bound [[Heterotrimeric G protein#Alpha subunits|G alpha]] subunits. Acting as a [[GTPase]] activating protein (GAP), the protein increases the rate of conversion of the GTP to [[guanosine diphosphate|GDP]]. This hydrolysis allows the G alpha subunits to bind [[Beta-gamma complex|G beta/gamma]] subunit heterodimers, forming inactive G-protein heterotrimers, thereby terminating the signal. Alternate transcriptional splice variants of this gene have been observed but have not been thoroughly characterized.<ref name="entrez"/>
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
Increasing the expression of the RGS14 protein in the [[Visual cortex#V2|V2 secondary visual cortex]] of mice promotes the conversion of short-term to long-term object-[[recognition memory]].<ref name="pmid19574389">{{cite journal | vauthors = López-Aranda MF, López-Téllez JF, Navarro-Lobato I, Masmudi-Martín M, Gutiérrez A, Khan ZU | title = Role of layer 6 of V2 visual cortex in object-recognition memory | journal = Science | volume = 325 | issue = 5936 | pages = 87–9 |date=July 2009 | pmid = 19574389 | doi = 10.1126/science.1170869 | laysummary = http://io9.com/5306489/a-drug-that-could-give-you-perfect-visual-memory | laysource = Mad Science }}</ref> Conversely RGS14 is enriched in [[Apical dendrite#CA2|CA2 pyramidal neurons]] and suppresses [[synaptic plasticity]] of these synapses and [[hippocampus|hippocampal]]-based learning and memory.<ref name="pmid20837545">{{cite journal | vauthors = Lee SE, Simons SB, Heldt SA, Zhao M, Schroeder JP, Vellano CP, Cowan DP, Ramineni S, Yates CK, Feng Y, Smith Y, Sweatt JD, Weinshenker D, Ressler KJ, Dudek SM, Hepler JR | title = RGS14 is a natural suppressor of both synaptic plasticity in CA2 neurons and hippocampal-based learning and memory | journal = Proc Natl Acad Sci U S A | volume = 107| issue = 39| pages = 16994–8|date=September 2010 | pmid = 20837545 | doi = 10.1073/pnas.1005362107 | laysummary = http://www.medicaldaily.com/news/20100918/2064/gene-limits-learning-and-memory-in-mice.htm | laysource = MedicalDaily | pmc=2947872}}</ref>
{{GNF_Protein_box
| image = PBB_Protein_RGS14_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1kjy.
| PDB = {{PDB2|1kjy}}, {{PDB2|2jnu}}
| Name = Regulator of G-protein signalling 14
| HGNCid = 9996
| Symbol = RGS14
| AltSymbols =;
| OMIM = 602513
| ECnumber =
| Homologene = 4735
| MGIid = 1859709
| GeneAtlas_image1 = PBB_GE_RGS14_38290_at_tn.png
| GeneAtlas_image2 = PBB_GE_RGS14_204280_at_tn.png
| GeneAtlas_image3 = PBB_GE_RGS14_211021_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005057 |text = receptor signaling protein activity}} {{GNF_GO|id=GO:0005096 |text = GTPase activator activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005819 |text = spindle}}
| Process = {{GNF_GO|id=GO:0007067 |text = mitosis}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0008277 |text = regulation of G-protein coupled receptor protein signaling pathway}} {{GNF_GO|id=GO:0009968 |text = negative regulation of signal transduction}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 10636
    | Hs_Ensembl = ENSG00000169220
    | Hs_RefseqProtein = NP_006471
    | Hs_RefseqmRNA = NM_006480
    | Hs_GenLoc_db =
    | Hs_GenLoc_chr = 5
    | Hs_GenLoc_start = 176717450
    | Hs_GenLoc_end = 176732204
    | Hs_Uniprot = O43566
    | Mm_EntrezGene = 51791
    | Mm_Ensembl = ENSMUSG00000052087
    | Mm_RefseqmRNA = XM_001004354
    | Mm_RefseqProtein = XP_001004354
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 13
    | Mm_GenLoc_start = 55379393
    | Mm_GenLoc_end = 55394309
    | Mm_Uniprot = Q8K2R4
  }}
}}
'''Regulator of G-protein signalling 14''', also known as '''RGS14''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RGS14 regulator of G-protein signalling 14| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10636| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
==Interactions==
{{PBB_Summary
RGS14 has been shown to [[Protein-protein interaction|interact]] with:
| section_title =  
* [[GNAI1]]<ref name="pmid11387333">{{cite journal | vauthors = Kimple RJ, De Vries L, Tronchère H, Behe CI, Morris RA, Gist Farquhar M, Siderovski DP | title = RGS12 and RGS14 GoLoco motifs are G alpha(i) interaction sites with guanine nucleotide dissociation inhibitor Activity | journal = J. Biol. Chem. | volume = 276 | issue = 31 | pages = 29275–81 |date=August 2001 | pmid = 11387333 | doi = 10.1074/jbc.M103208200 | url = | issn = }}</ref><ref name="pmid11739605">{{cite journal | vauthors = Hollinger S, Taylor JB, Goldman EH, Hepler JR | title = RGS14 is a bifunctional regulator of Galphai/o activity that exists in multiple populations in brain | journal = J. Neurochem. | volume = 79 | issue = 5 | pages = 941–9 |date=December 2001 | pmid = 11739605 | doi = 10.1046/j.1471-4159.2001.00629.x| url = | issn = }}</ref><ref name="pmid11976690">{{cite journal | vauthors = Kimple RJ, Kimple ME, Betts L, Sondek J, Siderovski DP | title = Structural determinants for GoLoco-induced inhibition of nucleotide release by Galpha subunits | journal = Nature | volume = 416 | issue = 6883 | pages = 878–81 |date=April 2002 | pmid = 11976690 | doi = 10.1038/416878a | url = | issn = }}</ref><ref name="pmid16870394">{{cite journal | vauthors = Shu FJ, Ramineni S, Amyot W, Hepler JR | title = Selective interactions between Gi alpha1 and Gi alpha3 and the GoLoco/GPR domain of RGS14 influence its dynamic subcellular localization | journal = Cell. Signal. | volume = 19 | issue = 1 | pages = 163–76 |date=January 2007 | pmid = 16870394 | doi = 10.1016/j.cellsig.2006.06.002 | url = | issn = }}</ref> and
| summary_text = This gene encodes a member of the regulator of G-protein signaling family. This protein contains one RGS domain, two Raf-like Ras-binding domains (RBDs), and one GoLoco domain. The protein attenuates the signaling activity of G-proteins by binding, through its GoLoco domain, to specific types of activated, GTP-bound G alpha subunits. Acting as a GTPase activating protein (GAP), the protein increases the rate of conversion of the GTP to GDP. This hydrolysis allows the G alpha subunits to bind G beta/gamma subunit heterodimers, forming inactive G-protein heterotrimers, thereby terminating the signal. Alternate transcriptional splice variants of this gene have been observed but have not been thoroughly characterized.<ref name="entrez">{{cite web | title = Entrez Gene: RGS14 regulator of G-protein signalling 14| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10636| accessdate = }}</ref>
* [[GNAI3]].<ref name=pmid11387333/>
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal | author=Snow BE, Antonio L, Suggs S, ''et al.'' |title=Molecular cloning and expression analysis of rat Rgs12 and Rgs14. |journal=Biochem. Biophys. Res. Commun. |volume=233 |issue= 3 |pages= 770-7 |year= 1997 |pmid= 9168931 |doi= 10.1006/bbrc.1997.6537 }}
*{{cite journal   |vauthors=Snow BE, Antonio L, Suggs S, etal |title=Molecular cloning and expression analysis of rat Rgs12 and Rgs14. |journal=Biochem. Biophys. Res. Commun. |volume=233 |issue= 3 |pages= 770–7 |year= 1997 |pmid= 9168931 |doi= 10.1006/bbrc.1997.6537 }}
*{{cite journal | author=Traver S, Bidot C, Spassky N, ''et al.'' |title=RGS14 is a novel Rap effector that preferentially regulates the GTPase activity of galphao. |journal=Biochem. J. |volume=350 Pt 1 |issue=  |pages= 19-29 |year= 2001 |pmid= 10926822 |doi=  }}
*{{cite journal   |vauthors=Traver S, Bidot C, Spassky N, etal |title=RGS14 is a novel Rap effector that preferentially regulates the GTPase activity of galphao. |journal=Biochem. J. |volume=350 |issue=  1|pages= 19–29 |year= 2001 |pmid= 10926822 |doi= 10.1042/0264-6021:3500019| pmc=1221220 }}
*{{cite journal | author=Cho H, Kozasa T, Takekoshi K, ''et al.'' |title=RGS14, a GTPase-activating protein for Gialpha, attenuates Gialpha- and G13alpha-mediated signaling pathways. |journal=Mol. Pharmacol. |volume=58 |issue= 3 |pages= 569-76 |year= 2000 |pmid= 10953050 |doi=  }}
*{{cite journal   |vauthors=Cho H, Kozasa T, Takekoshi K, etal |title=RGS14, a GTPase-activating protein for Gialpha, attenuates Gialpha- and G13alpha-mediated signaling pathways. |journal=Mol. Pharmacol. |volume=58 |issue= 3 |pages= 569–76 |year= 2000 |pmid= 10953050 |doi=  }}
*{{cite journal  | author=Kimple RJ, De Vries L, Tronchère H, ''et al.'' |title=RGS12 and RGS14 GoLoco motifs are G alpha(i) interaction sites with guanine nucleotide dissociation inhibitor Activity. |journal=J. Biol. Chem. |volume=276 |issue= 31 |pages= 29275-81 |year= 2001 |pmid= 11387333 |doi= 10.1074/jbc.M103208200 }}
*{{cite journal  | vauthors=Hollinger S, Taylor JB, Goldman EH, Hepler JR |title=RGS14 is a bifunctional regulator of Gi/oalpha activity that exists in multiple populations in brain. |journal=Journal of Neurochemistry |volume=79 |issue= 5 |pages= 941–49 |year= 2001 |pmid= 11739605 |doi=10.1046/j.1471-4159.2001.00629.x  }}
*{{cite journal | author=Sierra DA, Gilbert DJ, Householder D, ''et al.'' |title=Evolution of the regulators of G-protein signaling multigene family in mouse and human. |journal=Genomics |volume=79 |issue= 2 |pages= 177-85 |year= 2002 |pmid= 11829488 |doi= 10.1006/geno.2002.6693 }}
*{{cite journal  |vauthors=Kimple RJ, De Vries L, Tronchère H, etal |title=RGS12 and RGS14 GoLoco motifs are G alpha(i) interaction sites with guanine nucleotide dissociation inhibitor Activity. |journal=J. Biol. Chem. |volume=276 |issue= 31 |pages= 29275–81 |year= 2001 |pmid= 11387333 |doi= 10.1074/jbc.M103208200 }}
*{{cite journal | author=Kimple RJ, Kimple ME, Betts L, ''et al.'' |title=Structural determinants for GoLoco-induced inhibition of nucleotide release by Galpha subunits. |journal=Nature |volume=416 |issue= 6883 |pages= 878-81 |year= 2002 |pmid= 11976690 |doi= 10.1038/416878a }}
*{{cite journal   |vauthors=Sierra DA, Gilbert DJ, Householder D, etal |title=Evolution of the regulators of G-protein signaling multigene family in mouse and human. |journal=Genomics |volume=79 |issue= 2 |pages= 177–85 |year= 2002 |pmid= 11829488 |doi= 10.1006/geno.2002.6693 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal   |vauthors=Kimple RJ, Kimple ME, Betts L, etal |title=Structural determinants for GoLoco-induced inhibition of nucleotide release by Galpha subunits. |journal=Nature |volume=416 |issue= 6883 |pages= 878–81 |year= 2002 |pmid= 11976690 |doi= 10.1038/416878a }}
*{{cite journal  | author=Hollinger S, Ramineni S, Hepler JR |title=Phosphorylation of RGS14 by protein kinase A potentiates its activity toward G alpha i. |journal=Biochemistry |volume=42 |issue= 3 |pages= 811-9 |year= 2003 |pmid= 12534294 |doi= 10.1021/bi026664y }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal  | vauthors=Hollinger S, Ramineni S, Hepler JR |title=Phosphorylation of RGS14 by protein kinase A potentiates its activity toward G alpha i. |journal=Biochemistry |volume=42 |issue= 3 |pages= 811–9 |year= 2003 |pmid= 12534294 |doi= 10.1021/bi026664y }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
*{{cite journal   |vauthors=Ota T, Suzuki Y, Nishikawa T, etal |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
*{{cite journal | author=Martin-McCaffrey L, Willard FS, Oliveira-dos-Santos AJ, ''et al.'' |title=RGS14 is a mitotic spindle protein essential from the first division of the mammalian zygote. |journal=Dev. Cell |volume=7 |issue= 5 |pages= 763-9 |year= 2004 |pmid= 15525537 |doi= 10.1016/j.devcel.2004.10.004 }}
*{{cite journal   |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 }}
*{{cite journal | author=Martin-McCaffrey L, Willard FS, Pajak A, ''et al.'' |title=RGS14 is a microtubule-associated protein. |journal=Cell Cycle |volume=4 |issue= 7 |pages= 953-60 |year= 2006 |pmid= 15917656 |doi=  }}
*{{cite journal   |vauthors=Martin-McCaffrey L, Willard FS, Oliveira-dos-Santos AJ, etal |title=RGS14 is a mitotic spindle protein essential from the first division of the mammalian zygote. |journal=Dev. Cell |volume=7 |issue= 5 |pages= 763–9 |year= 2004 |pmid= 15525537 |doi= 10.1016/j.devcel.2004.10.004 }}
*{{cite journal | author=Rual JF, Venkatesan K, Hao T, ''et al.'' |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173-8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 }}
*{{cite journal   |vauthors=Martin-McCaffrey L, Willard FS, Pajak A, etal |title=RGS14 is a microtubule-associated protein. |journal=Cell Cycle |volume=4 |issue= 7 |pages= 953–60 |year= 2006 |pmid= 15917656 |doi=  10.4161/cc.4.7.1787}}
*{{cite journal   |vauthors=Rual JF, Venkatesan K, Hao T, etal |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 }}
*{{cite journal  | vauthors=Shu  FJ, Ramineni S, Amyot  W, Hepler  JR |title=Selective interactions between Gialpha1 and Gialpha3 and the GoLoco/GPR domain of RGS14 influence its dynamic subcellular localization. |journal=Cellular Signalling |volume=19 |issue= 1 |pages= 941–49 |year= 2007 |pmid= 16870394 |doi=10.1016/j.cellsig.2006.06.002  }}
*{{cite journal  | vauthors=Shu FJ, Ramineni S, Hepler JR  |title=RGS14 is multifunctional scaffold that integrates G protein and Ras/Raf MAPkinase signaling pathways. |journal=Cellular Signalling |volume= |issue=  |pages= in press |year= 2009 |pmid=  |doi=  }}
 
}}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=10636}}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = no
| update_citations = yes
}}


{{protein-stub}}
{{gene-5-stub}}
{{WikiDoc Sources}}

Latest revision as of 03:52, 9 September 2018

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Regulator of G-protein signaling 14 (RGS14) is a protein that in humans is encoded by the RGS14 gene.[1]

Function

RGS14 is a member of the regulator of G protein signalling family. This protein contains one RGS domain, two Raf-like Ras-binding domains (RBDs), and one GoLoco motif. The protein attenuates the signaling activity of G-proteins by binding, through its GoLoco domain, to specific types of activated, GTP-bound G alpha subunits. Acting as a GTPase activating protein (GAP), the protein increases the rate of conversion of the GTP to GDP. This hydrolysis allows the G alpha subunits to bind G beta/gamma subunit heterodimers, forming inactive G-protein heterotrimers, thereby terminating the signal. Alternate transcriptional splice variants of this gene have been observed but have not been thoroughly characterized.[1]

Increasing the expression of the RGS14 protein in the V2 secondary visual cortex of mice promotes the conversion of short-term to long-term object-recognition memory.[2] Conversely RGS14 is enriched in CA2 pyramidal neurons and suppresses synaptic plasticity of these synapses and hippocampal-based learning and memory.[3]

Interactions

RGS14 has been shown to interact with:

References

  1. 1.0 1.1 "Entrez Gene: RGS14 regulator of G-protein signalling 14".
  2. López-Aranda MF, López-Téllez JF, Navarro-Lobato I, Masmudi-Martín M, Gutiérrez A, Khan ZU (July 2009). "Role of layer 6 of V2 visual cortex in object-recognition memory". Science. 325 (5936): 87–9. doi:10.1126/science.1170869. PMID 19574389. Lay summaryMad Science.
  3. Lee SE, Simons SB, Heldt SA, Zhao M, Schroeder JP, Vellano CP, Cowan DP, Ramineni S, Yates CK, Feng Y, Smith Y, Sweatt JD, Weinshenker D, Ressler KJ, Dudek SM, Hepler JR (September 2010). "RGS14 is a natural suppressor of both synaptic plasticity in CA2 neurons and hippocampal-based learning and memory". Proc Natl Acad Sci U S A. 107 (39): 16994–8. doi:10.1073/pnas.1005362107. PMC 2947872. PMID 20837545. Lay summaryMedicalDaily.
  4. 4.0 4.1 Kimple RJ, De Vries L, Tronchère H, Behe CI, Morris RA, Gist Farquhar M, Siderovski DP (August 2001). "RGS12 and RGS14 GoLoco motifs are G alpha(i) interaction sites with guanine nucleotide dissociation inhibitor Activity". J. Biol. Chem. 276 (31): 29275–81. doi:10.1074/jbc.M103208200. PMID 11387333.
  5. Hollinger S, Taylor JB, Goldman EH, Hepler JR (December 2001). "RGS14 is a bifunctional regulator of Galphai/o activity that exists in multiple populations in brain". J. Neurochem. 79 (5): 941–9. doi:10.1046/j.1471-4159.2001.00629.x. PMID 11739605.
  6. Kimple RJ, Kimple ME, Betts L, Sondek J, Siderovski DP (April 2002). "Structural determinants for GoLoco-induced inhibition of nucleotide release by Galpha subunits". Nature. 416 (6883): 878–81. doi:10.1038/416878a. PMID 11976690.
  7. Shu FJ, Ramineni S, Amyot W, Hepler JR (January 2007). "Selective interactions between Gi alpha1 and Gi alpha3 and the GoLoco/GPR domain of RGS14 influence its dynamic subcellular localization". Cell. Signal. 19 (1): 163–76. doi:10.1016/j.cellsig.2006.06.002. PMID 16870394.

Further reading