regulator of G-protein signaling 14

Target not currently curated in GtoImmuPdb

Target id: 2820

Nomenclature: regulator of G-protein signaling 14

Abbreviated Name: RGS14

Gene and Protein Information
Species	TM	AA	Chromosomal Location	Gene Symbol	Gene Name	Reference
Human	-	566	5q35.3	RGS14	regulator of G protein signaling 14
Mouse	-	547	13 29.8 cM	Rgs14	regulator of G-protein signaling 14
Rat	-	544	17p14	Rgs14	regulator of G-protein signaling 14

Previous and Unofficial Names
A28-RGS14 \| RGS-r \| RPIP1

Database Links
Alphafold	O43566 (Hs), P97492 (Mm), O08773 (Rn)
CATH/Gene3D	1.10.196.10
Ensembl Gene	ENSG00000169220 (Hs), ENSMUSG00000052087 (Mm), ENSRNOG00000015616 (Rn)
Entrez Gene	10636 (Hs), 51791 (Mm), 114705 (Rn)
Human Protein Atlas	ENSG00000169220 (Hs)
KEGG Gene	hsa:10636 (Hs), mmu:51791 (Mm), rno:114705 (Rn)
OMIM	602513 (Hs)
Pharos	O43566 (Hs)
RefSeq Nucleotide	NM_006480 (Hs), NM_016758 (Mm), NM_053764 (Rn)
RefSeq Protein	NP_006471 (Hs), NP_058038 (Mm), NP_446216 (Rn)
UniProtKB	O43566 (Hs), P97492 (Mm), O08773 (Rn)
Wikipedia	RGS14 (Hs)

Associated Proteins

G Proteins
Name	References
Gαi0	7,15,17-18,24,33

Interacting Proteins
Name	Effect	References
Gai1-GDP; Gai3-GDP	High affinity binding to the GPR motif resulting in RGS14 localization to the plasma membrane	17-18,33
α_2A-adrenoceptor	A preformed Gai1-GDP:RGS14 complex interacts with the receptor and is uncoupled by agonist activation of receptor	35-36
Gai/o-GTP	Binding to the RGS domain resulting in accelerated Ga-GTP hydrolysis	7,17-18,32
Rap2A-GTP; Rap1-GTP	Binding to the R1 Ras/Rap-binding domain (RBD)	32
H-Ras-GTP	Binding to the R1 Ras/Rap-binding domain (RBD)	28,35,38
regulator of G-protein signaling 4	RGS4 and RGS5: Binding of RGS4 within the tandem R1-R2 RBD region enhances RGS activity of RGS4 towards Gai2-GTP	15,39
Raf kinases (Raf-1, B-Raf, A-Raf)	Specific binding site uncertain, with unknown consequences	28,38
Resistance to cholinesterase 8A (Ric-8A)	The non-receptor guanine nucleotide exchange factor (GEF) Ric-8A stimulates dissociation of a RGS14:Gαi1-GDP complex to form a stable Ric-8A-Gαi complex in the absence of GTP	35,37
NHERF1	Human/primate RGS14 has a carboxy-terminal extension that encodes a Type I PDZ ligand, like NHERF1. RGS14 binds to NHERF1 through its PDZ2 domain.	12
4-3-3γ	RGS14 binds to regulatory protein 14-3-3γ at two distinct sites. RGS14 phosphorylation-dependent interaction to 14-3-3γ at Ser28 inhibits interaction with active Gαi–AlF4⁻ to the RGS domain. RGS14:14-3-γ phosphorylation independent interaction inhibits RGS14 nuclear import.	14
Calcium/Calmodulin(Ca²⁺/CaM) and CaM Kinase II (CaMKII)	RGS14 directly binds to Ca²⁺/CaM and is phosphorylated by CaMKII in vitro. RGS14 associates with CaMKII and CaM in hippocampal CA2 neurons.	9

Associated Protein Comments

RGS14 has two distinct G protein binding sites, the RGS domain and the GPR motif (also known as GoLoco). The RGS domain can bind and serve as a GTPase activating protein (GAP) for activated (GTP bound) members of the Gα-i/o subfamily of G proteins including Gai1, Gai2, Gai3 and Gao. The GPR motif selectively binds inactive (GDP bound) Gai1 and Gai3.

Tissue Distribution

Brain, CA2 hippocampus, caudate

Species:	Human
Technique:	In situ hybridization, immunoperoxidase
References:	1,30

Heart (human and mouse)

Species:	Human
Technique:	Western blot
References:	20

Brain, temporal lobe, spleen, lymphocytes, kidney

Species:	Human
Technique:	In situ hybridization, Western blot
References:	8

Kidney proximal and distal tubule cells

Species:	Human
Technique:	Western Blot, immunofluorescent staining
References:	12

Brain (area CA2 hippocampus)

Species:	Mouse
Technique:	Immunocytochemistry, in situ hybridisation, Western blot
References:	10,19,32

Brain: piriform cortex, olfactory regions, neocortical layers (II, III, and V), hippocampus, striatum, neurons in hippocampal area CA2

Species:	Mouse
Technique:	Immunoperoxidase labeling, immunoblot, proteomic analysis, blue native-PAGE
References:	9-10,13

Brain (hippocampus), lung, spleen, heart

Species:	Rat
Technique:	Immunocytochemistry, Western blot
References:	17,29,32

Neuroblastoma B35 cell line

Species:	Rat
Technique:	SDS-Page, immunoblot, confocal imaging and 3D-structured illumination microscopy
References:	2

Brain: hippocampus (CA2 and CA1 region), basal ganglia, amygdala, caudate nucleus, putamen, substantia nigra pars reticulata, globus pallidus

Species:	Monkey
Technique:	Immunoblot analysis, electron microscopy
References:	30

Tissue Distribution Comments

Levels of messenger RNA that encode for this protein are detectable in most tissues by RT-PCR. However, detectable protein expression is very limited.

Functional Assays

Intracellular translocation assay using immunocytochemistry-ICC

Species:	Rat
Tissue:	RGS14 translocation from cytosol to the plasma membrane or to nucleus.
Response measured:	HeLa cells
References:	6,27

GTPase activating protein (GAP)

Species:	Rat
Tissue:	Pure protein
Response measured:	Marked enhancement of Gai/o GTPase activity in single-turnover assays; enhancement of receptor-stimulated steady state GTPase activity of Gai2.
References:	7,15,17,25

Guanine nucleotide dissociation inhibition (GDI)

Species:	Rat
Tissue:	Pure protein
Response measured:	RGS14 inhibits GDP release for Gai1.
References:	17-18,25

Bioluminesence Resonance Energy Transfer (BRET)

Species:	Rat
Tissue:	HEK293 cells (human)
Response measured:	RGS14 interactions with active and inactive Gai1, active Gao, and H-Ras-GTP in live cells.
References:	3-4,35

Activity-induced long-term potentation (LTP)

Species:	Mouse
Tissue:	CA2 hippocampal neurons of hippocampal slices
Response measured:	Loss of RGS14 (RGS14-KO) results in nascent robust LTP in proximal dendrites of CA2 neurons.
References:	19

Co-expression of RGS14 with the Cav1.2 calcium channel in HEK cells

Species:	None
Tissue:	HEK293 cells (human)
Response measured:	Partial inhibition of Cav1.2 calcium currents
References:	23

RGS14 Inhibition of ERK activation

Species:	Rat
Tissue:	HeLa cells
Response measured:	RGS14 inhibits PDGF-stimulated ERK phosphorylation.
References:	28

Kinetic Bioluminescence Resonance Energy Transfer (Kinetic BRET)

Species:	None
Tissue:	HEK293T cells
Response measured:	G protein activation and deactivation kinetics by RGS14 in response to GPCR agonist/antagonist treatment in live cells.
References:	5

Field Potential Recordings and LTP protocol

Species:	Mouse
Tissue:	CA2 pyramidal neurons, hippocampal brain slice
Response measured:	Synaptic potentiation in area CA2 in the presence or absence of RSG14 in brain.
References:	11

Activity-dependent spine structural plasticity (sLTP) using two-photon fluorescent microscopy

Species:	Mouse
Tissue:	CA1 and CA2 dendritic spines
Response measured:	Dendritic spine volume change following repetitive glutamate uncaging to induce sLTP comparing RGS14 WT CA2, RGS14 KO CA2, and CA1 controls.
References:	11

Phosphate transport

Species:	Human
Tissue:	Kidney cells, RPTEC (human renal proximal tubule epithelial immortalized) cells
Response measured:	PTH induced phosphate uptake in the presence or absence of RGS14.
References:	12

Physiological Functions

Natural suppressor of hippocampal (CA2)-based learning and memory

Species:	Mouse
Tissue:	Freely moving whole animal
References:	19

Suppression of long-term potentiation in CA2 neurons

Species:	Mouse
Tissue:	CA2 neurons
References:	19

Human RGS14 inhibits PTH-sensitive phosphate uptake in human kidney cells

Species:	Human
Tissue:	Human renal proximal tubule cells
References:	12

RGS14 attenuates the development of cardiac remodeling through MEK–ERK1/2 signaling

Species:	Mouse
Tissue:	Cardiomyocytes
References:	20

Disruption of RGS14 protein expression by genetic knockout in mice extends their lifespan and has multiple beneficial effects related to healthful aging

Species:	Mouse
Tissue:	Brown adipose tissue, skeletal muscle
References:	34

RGS14 negatively regulates the long-term structural plasticity of dendritic spines of CA2 neurons by limiting postsynaptic calcium signaling

Species:	Mouse
Tissue:	Dendritic spines
References:	11

Physiological Consequences of Altering Gene Expression

Mice engineered to lack RGS14 perform significantly better than paired wild-type litter mates in tests of hippocampal-mediated spatial learning (Morris Water maze) and memory (novel object recognition) with no changes in non-hippocampal behaviors.

Species:	Mouse
Tissue:	Freely moving whole animal
Technique:	Gene knockout
References:	19

RGS14 is not naturally expressed in visual cortex. However, ectopic over-expression of recombinant RGS14 in neurons of layer 6 of V2 visual secondary visual cortex promoted the conversion of a normal short-term object-recognition memory (45 minutes) into long-term memory detectable even after many months.

Species:	Rat
Tissue:	Visual cortex
Technique:	Viral gene transfer
References:	21

Disruption of RGS14 resulted in pathological cardiac remodeling response. Overexpression of RGS14 alleviated the cardiac hypertrophy and dysfunction induced by aortic banding operation. RGS14 mediates cardio protection by regulating the MEK–ERK1/2 signaling pathway.

Species:	Mouse
Tissue:	Heart tissue, cardiomyocytes
Technique:	Generation of RGS14 KO mice, transgenic mice with RGS14 overexpression
References:	20

Disruption of RGS14 protein expression by genetic knockout in mice extends their lifespan and has multiple beneficial effects related to healthful aging

Species:	Mouse
Tissue:	Brown adipose tissue, skeletal muscle
Technique:
References:	34

Physiological Consequences of Altering Gene Expression Comments

One study [22] reports that knock-out of RGS14 is embryonic lethal. However, other studies [26] suggests this is an artifact of the method (PGK-neo) used to generate the aforementioned KO mouse. This study shows that use of PGK-neo results in unexpected phenotypes including embryonic lethality that reflect more than just the loss of function of the targeted gene.

Biologically Significant Variants

Type:	Point mutation
Species:	Rat
Description:	Point mutation within the R1 domain of Rgs14 significantly reduces interactions with active H-Ras-GTP and Rap2-GTP.
Amino acid change:	Arg333Leu (R333L)
References:	28,33

Type:	Point mutation
Species:	Rat
Description:	Double point mutations within the RGS domain of Rgs14 blocks interactions with Gai/o-GTP and prevents RGS activity.
Amino acid change:	Glu92Ala (E92A) plus Asn93>Ala (N93A)
References:	7,27,33,36

Type:	Point mutation
Species:	Rat
Description:	Thr494Ala (T494A) substitution mutation adjacent to the GPR/GoLoco motif prevents phosphoylation of this residue of Rgs14 by protein kinase A (PKA), whereas a Thr494Glu substitution mutation mimics phosphorylation at this site and increases Rgs14 affinity for Gai1 binding 3-fold.
Amino acid change:	Thr494Ala (T494A)
References:	16

Type:	Point mutation
Species:	Mouse
Description:	Mutating Leu506>Ala plus Leu507>Ala (LL/AA) within a defined nucelar export signal (NES) on Rgs14 causes Rgs14 to accumulate in the nucleus.
Amino acid change:	Leu506Ala (L506A) plus Leu507Ala (L507A)
References:	6,27

Type:	Point mutation
Species:	Rat
Description:	Double point mutation within the GPR/GoLoco motif blocks interactions with Gai/o-GDP.
Amino acid change:	Gln515Ala (Q515A) plus Glu516Ala (E516A)
References:	27,33,36

Type:	Point mutation
Species:	Human
Description:	Several rare human variants have been noted at positions Asp563 and Ala565 in the PDZ-binding motif/ligand of human RGS14. Variant Asp563Asn blocked RGS14 binding to NHERF1 and blocked RGS14 inhibition of PTH-senstive phsopahte uptake in renal proximal tubule cells. Replacement of Asp563 by Gly maintained binding. Substitution of Ala565 by Ser and Val also bind to NHERF1.
Amino acid change:	Asp53Asn, Asp563Gly, Ala565Ser, Ala565Val
References:	12

Type:	Point mutation
Species:	Rat
Description:	To determine the 14-3-3γ binding site on RGS14, three mutations were generated: Ser258Ala, Ser286Ala, and Ser218Ala. Mutations at 258 and 286 had no effect on 14-3-3γ binding to RGS14. However, Ser218Ala shows decreased association between RGS14 and 14-3-3γ.
Amino acid change:	Ser258Ala, Ser286Ala, and Ser218Ala
References:	14

Type:	Point mutation
Species:	Human
Description:	Two reported human genetic variants, L505R (LR) and R507Q (RQ) are located within the nuclear export sequence (NES) of human RGS14. Protein carrying LR or RQ redirects RGS14 from dendritic spines to the nucleus of host neurons, and disinhibits activity induced LTP in hippocampal neurons.
Amino acid change:	Leu505Arg, Arg507Gln
References:	31

General Comments

To date, there is no reported protein crystal structure for full-length RGS14. However, structural data has been reported for isolated domains of RGS14 (X-ray and NMR) or full-length protein (hydrogen-deuterium exchange, HDX). This includes:
1) X-ray protein crystal data for human Gai1-GDP bound to a peptide corresponding to the GPR/GoLoco motif of rat Rgs14 (PDB 1KJY)
2) NMR data for the isolated RGS domain of human RGS14 (PDB 2JNU)
3) NMR data for the isolated RBD2 domain of mouse Rgs14 (PDB 1WFY)
4) HDX data for full-length RGS14 alone (apo RGS14) and RGS14 bound to either Gao-AlF4-, Gai1-GDP, or both has been reported [4].

References

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1. Allen Brain Atlas. RGS14. Accessed on 21/06/2016. Modified on 21/06/2016. Allen Brain Atlas, http://human.brain-map.org/microarray/search/show?exact_match=false&search_term=RGS14&search_type=gene

2. Branch MR, Hepler JR. (2017) Endogenous RGS14 is a cytoplasmic-nuclear shuttling protein that localizes to juxtanuclear membranes and chromatin-rich regions of the nucleus. PLoS One, 12 (9): e0184497. [PMID:28934222]

3. Brown NE, Blumer JB, Hepler JR. (2015) Bioluminescence resonance energy transfer to detect protein-protein interactions in live cells. Methods Mol Biol, 1278: 457-65. [PMID:25859969]

4. Brown NE, Goswami D, Branch MR, Ramineni S, Ortlund EA, Griffin PR, Hepler JR. (2015) Integration of G protein α (Gα) signaling by the regulator of G protein signaling 14 (RGS14). J Biol Chem, 290 (14): 9037-49. [PMID:25666614]

5. Brown NE, Lambert NA, Hepler JR. (2016) RGS14 regulates the lifetime of Gα-GTP signaling but does not prolong Gβγ signaling following receptor activation in live cells. Pharmacol Res Perspect, 4 (5): e00249. [PMID:27713821]

6. Cho H, Kim DU, Kehrl JH. (2005) RGS14 is a centrosomal and nuclear cytoplasmic shuttling protein that traffics to promyelocytic leukemia nuclear bodies following heat shock. J Biol Chem, 280 (1): 805-14. [PMID:15520006]

7. Cho H, Kozasa T, Takekoshi K, De Gunzburg J, Kehrl JH. (2000) RGS14, a GTPase-activating protein for Gialpha, attenuates Gialpha- and G13alpha-mediated signaling pathways. Mol Pharmacol, 58 (3): 569-76. [PMID:10953050]

8. EMBL-EBI Expression Atlas. RGS14 regulator of G-protein signaling 14. Accessed on 21/06/2016. Modified on 21/06/2016. EMBL-EBI Expression Atlas, http://www.ebi.ac.uk/gxa/genes/ENSG00000169220

9. Evans PR, Gerber KJ, Dammer EB, Duong DM, Goswami D, Lustberg DJ, Zou J, Yang JJ, Dudek SM, Griffin PR et al.. (2018) Interactome Analysis Reveals Regulator of G Protein Signaling 14 (RGS14) is a Novel Calcium/Calmodulin (Ca²⁺/CaM) and CaM Kinase II (CaMKII) Binding Partner. J Proteome Res, 17 (4): 1700-1711. [PMID:29518331]

10. Evans PR, Lee SE, Smith Y, Hepler JR. (2014) Postnatal developmental expression of regulator of G protein signaling 14 (RGS14) in the mouse brain. J Comp Neurol, 522 (1): 186-203. [PMID:23817783]

11. Evans PR, Parra-Bueno P, Smirnov MS, Lustberg DJ, Dudek SM, Hepler JR, Yasuda R. (2018) RGS14 Restricts Plasticity in Hippocampal CA2 by Limiting Postsynaptic Calcium Signaling. eNeuro, 5 (3). [PMID:29911178]

12. Friedman PA, Mamonova T, Magyar CE, Squires KE, Sneddon WB, Emlet DR, Hepler JR. (2019) Genetic variants disrupt human RGS14 binding to NHERF1 and regulation of NPT2A-mediated phosphate transport. bioRxiv, Preprint. DOI: doi.org/10.1101/540781

13. Gerber KJ, Dammer EB, Duong DM, Deng Q, Dudek SM, Seyfried NT, Hepler JR. (2019) Specific Proteomes of Hippocampal Regions CA2 and CA1 Reveal Proteins Linked to the Unique Physiology of Area CA2. J Proteome Res, 18 (6): 2571-2584. [PMID:31059263]

14. Gerber KJ, Squires KE, Hepler JR. (2018) 14-3-3γ binds regulator of G protein signaling 14 (RGS14) at distinct sites to inhibit the RGS14:Gα_i-AlF₄^- signaling complex and RGS14 nuclear localization. J Biol Chem, 293 (38): 14616-14631. [PMID:30093406]

15. Hepler JR, Cladman W, Ramineni S, Hollinger S, Chidiac P. (2005) Novel activity of RGS14 on Goalpha and Gialpha nucleotide binding and hydrolysis distinct from its RGS domain and GDI activity. Biochemistry, 44 (14): 5495-502. [PMID:15807543]

16. Hollinger S, Ramineni S, Hepler JR. (2003) Phosphorylation of RGS14 by protein kinase A potentiates its activity toward G alpha i. Biochemistry, 42 (3): 811-9. [PMID:12534294]

17. Hollinger S, Taylor JB, Goldman EH, Hepler JR. (2001) RGS14 is a bifunctional regulator of Galphai/o activity that exists in multiple populations in brain. J Neurochem, 79 (5): 941-9. [PMID:11739605]

18. Kimple RJ, De Vries L, Tronchère H, Behe CI, Morris RA, Gist Farquhar M, Siderovski DP. (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. [PMID:11387333]

19. Lee SE, Simons SB, Heldt SA, Zhao M, Schroeder JP, Vellano CP, Cowan DP, Ramineni S, Yates CK, Feng Y et al.. (2010) RGS14 is a natural suppressor of both synaptic plasticity in CA2 neurons and hippocampal-based learning and memory. Proc Natl Acad Sci USA, 107 (39): 16994-8. [PMID:20837545]

20. Li Y, Tang XH, Li XH, Dai HJ, Miao RJ, Cai JJ, Huang ZJ, Chen AF, Xing XW, Lu Y et al.. (2016) Regulator of G protein signalling 14 attenuates cardiac remodelling through the MEK-ERK1/2 signalling pathway. Basic Res Cardiol, 111 (4): 47. [PMID:27298141]

21. López-Aranda MF, López-Téllez JF, Navarro-Lobato I, Masmudi-Martín M, Gutiérrez A, Khan ZU. (2009) Role of layer 6 of V2 visual cortex in object-recognition memory. Science, 325 (5936): 87-9. [PMID:19574389]

22. Martin-McCaffrey L, Willard FS, Oliveira-dos-Santos AJ, Natale DR, Snow BE, Kimple RJ, Pajak A, Watson AJ, Dagnino L, Penninger JM et al.. (2004) RGS14 is a mitotic spindle protein essential from the first division of the mammalian zygote. Dev Cell, 7 (5): 763-9. [PMID:15525537]

23. Martín-Montañez E, Acevedo MJ, López-Téllez JF, Duncan RS, Mateos AG, Pavía J, Koulen P, Khan ZU. (2010) Regulator of G-protein signaling 14 protein modulates Ca²+ influx through Cav1 channels. Neuroreport, 21 (16): 1034-9. [PMID:20842066]

24. Mittal V, Linder ME. (2004) The RGS14 GoLoco domain discriminates among Galphai isoforms. J Biol Chem, 279 (45): 46772-8. [PMID:15337739]

25. Mittal V, Linder ME. (2006) Biochemical characterization of RGS14: RGS14 activity towards G-protein alpha subunits is independent of its binding to Rap2A. Biochem J, 394 (Pt 1): 309-15. [PMID:16246175]

26. Scacheri PC, Crabtree JS, Novotny EA, Garrett-Beal L, Chen A, Edgemon KA, Marx SJ, Spiegel AM, Chandrasekharappa SC, Collins FS. (2001) Bidirectional transcriptional activity of PGK-neomycin and unexpected embryonic lethality in heterozygote chimeric knockout mice. Genesis, 30 (4): 259-63. [PMID:11536432]

27. Shu FJ, Ramineni S, Amyot W, Hepler JR. (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. [PMID:16870394]

28. Shu FJ, Ramineni S, Hepler JR. (2010) RGS14 is a multifunctional scaffold that integrates G protein and Ras/Raf MAPkinase signalling pathways. Cell Signal, 22 (3): 366-76. [PMID:19878719]

29. Snow BE, Antonio L, Suggs S, Gutstein HB, Siderovski DP. (1997) Molecular cloning and expression analysis of rat Rgs12 and Rgs14. Biochem Biophys Res Commun, 233 (3): 770-7. [PMID:9168931]

30. Squires KE, Gerber KJ, Pare JF, Branch MR, Smith Y, Hepler JR. (2018) Regulator of G protein signaling 14 (RGS14) is expressed pre- and postsynaptically in neurons of hippocampus, basal ganglia, and amygdala of monkey and human brain. Brain Struct Funct, 223 (1): 233-253. [PMID:28776200]

31. Squires KE, Gerber KJ, Tillman MC, Lustberg DJ, Montañez-Miranda C, Zhao M, Ramineni S, Scharer CD, Shu F-j, Schroeder JP et al.. (2020) Human genetic variants disrupt RGS14 nuclear shuttling and regulation of LTP in hippocampal neurons. bioRxiv, Preprint. DOI: 10.1101/2020.09.10.289991

32. Traver S, Bidot C, Spassky N, Baltauss T, De Tand MF, Thomas JL, Zalc B, Janoueix-Lerosey I, Gunzburg JD. (2000) RGS14 is a novel Rap effector that preferentially regulates the GTPase activity of galphao. Biochem J, 350 Pt 1: 19-29. [PMID:10926822]

33. Traver S, Splingard A, Gaudriault G, De Gunzburg J. (2004) The RGS (regulator of G-protein signalling) and GoLoco domains of RGS14 co-operate to regulate Gi-mediated signalling. Biochem J, 379 (Pt 3): 627-32. [PMID:15112653]

34. Vatner DE, Zhang J, Oydanich M, Guers J, Katsyuba E, Yan L, Sinclair D, Auwerx J, Vatner SF. (2018) Enhanced longevity and metabolism by brown adipose tissue with disruption of the regulator of G protein signaling 14. Aging Cell, 17 (4): e12751. [PMID:29654651]

35. Vellano CP, Brown NE, Blumer JB, Hepler JR. (2013) Assembly and function of the regulator of G protein signaling 14 (RGS14)·H-Ras signaling complex in live cells are regulated by Gαi1 and Gαi-linked G protein-coupled receptors. J Biol Chem, 288 (5): 3620-31. [PMID:23250758]

36. Vellano CP, Maher EM, Hepler JR, Blumer JB. (2011) G protein-coupled receptors and resistance to inhibitors of cholinesterase-8A (Ric-8A) both regulate the regulator of g protein signaling 14 RGS14·Gαi1 complex in live cells. J Biol Chem, 286 (44): 38659-69. [PMID:21880739]

37. Vellano CP, Shu FJ, Ramineni S, Yates CK, Tall GG, Hepler JR. (2011) Activation of the regulator of G protein signaling 14-Gαi1-GDP signaling complex is regulated by resistance to inhibitors of cholinesterase-8A. Biochemistry, 50 (5): 752-62. [PMID:21158412]

38. Willard FS, Willard MD, Kimple AJ, Soundararajan M, Oestreich EA, Li X, Sowa NA, Kimple RJ, Doyle DA, Der CJ et al.. (2009) Regulator of G-protein signaling 14 (RGS14) is a selective H-Ras effector. PLoS ONE, 4 (3): e4884. [PMID:19319189]

39. Zhao P, Nunn C, Ramineni S, Hepler JR, Chidiac P. (2013) The Ras-binding domain region of RGS14 regulates its functional interactions with heterotrimeric G proteins. J Cell Biochem, 114 (6): 1414-23. [PMID:23255434]

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