RGS14

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RGS14
Protein RGS14 PDB 1kjy.png
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesRGS14, regulator of G protein signaling 14
External IDsOMIM: 602513 MGI: 1859709 HomoloGene: 4735 GeneCards: RGS14
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_006480
NM_001366617
NM_001366618

NM_016758
NM_001360714

RefSeq (protein)

NP_006471
NP_001353546
NP_001353547

NP_058038
NP_001347643

Location (UCSC)Chr 5: 177.36 – 177.37 MbChr 13: 55.52 – 55.53 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Regulator of G-protein signaling 14 (RGS14) is a protein that in humans is encoded by the RGS14 gene.[5]

Function[]

RGS14 is a member of the regulator of G protein signalling family. This protein contains one , 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.[5]

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.[6] Conversely RGS14 is enriched in CA2 pyramidal neurons and suppresses synaptic plasticity of these synapses and hippocampal-based learning and memory.[7]

Interactions[]

RGS14 has been shown to interact with:

References[]

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000169220 - Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000052087 - Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b "Entrez Gene: RGS14 regulator of G-protein signalling 14".
  6. ^ 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. Bibcode:2009Sci...325...87L. doi:10.1126/science.1170869. PMID 19574389. S2CID 23990759. Lay summaryMad Science. {{cite journal}}: Cite uses deprecated parameter |lay-url= (help)
  7. ^ 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. Bibcode:2010PNAS..10716994L. doi:10.1073/pnas.1005362107. PMC 2947872. PMID 20837545. Lay summaryMedicalDaily. {{cite journal}}: Cite uses deprecated parameter |lay-url= (help)
  8. ^ a b 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.
  9. ^ 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. S2CID 22913974.
  10. ^ 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. Bibcode:2002Natur.416..878K. doi:10.1038/416878a. PMID 11976690. S2CID 4406208.
  11. ^ 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[]

External links[]

  • Overview of all the structural information available in the PDB for UniProt: O43566 (Regulator of G-protein signaling 14) at the PDBe-KB.


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