RGS14
Template:PBB 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
- ^ a b "Entrez Gene: RGS14 regulator of G-protein signalling 14".
- ^ 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.
{{cite journal}}: Unknown parameter|laysource=ignored (help); Unknown parameter|laysummary=ignored (help)CS1 maint: multiple names: authors list (link) - ^ 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.
{{cite journal}}: Unknown parameter|laysource=ignored (help); Unknown parameter|laysummary=ignored (help)CS1 maint: multiple names: authors list (link) - ^ 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.
{{cite journal}}: CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link) - ^ 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.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ 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.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ 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.
{{cite journal}}: CS1 maint: multiple names: authors list (link)
Further reading
PDB gallery | |
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![1kjy: Crystal Structure of Human G[alpha]i1 Bound to the GoLoco Motif of RGS14](/wiki/File:PDB_1kjy_EBI.jpg)
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