Radixin: Difference between revisions

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{{Infobox_gene}}
{{PBB_Controls
'''Radixin''' is a [[protein]] that in humans is encoded by the ''RDX'' [[gene]].<ref name="pmid8486357">{{cite journal | vauthors = Wilgenbus KK, Milatovich A, Francke U, Furthmayr H | title = Molecular cloning, cDNA sequence, and chromosomal assignment of the human radixin gene and two dispersed pseudogenes | journal = Genomics | volume = 16 | issue = 1 | pages = 199–206 | date = June 1993 | pmid = 8486357 | pmc =  | doi = 10.1006/geno.1993.1159 }}</ref><ref name="pmid17226784">{{cite journal | vauthors = Khan SY, Ahmed ZM, Shabbir MI, Kitajiri S, Kalsoom S, Tasneem S, Shayiq S, Ramesh A, Srisailpathy S, Khan SN, Smith RJ, Riazuddin S, Friedman TB, Riazuddin S | title = Mutations of the RDX gene cause nonsyndromic hearing loss at the DFNB24 locus | journal = Hum Mutat | volume = 28 | issue = 5 | pages = 417–23 | date = April 2007 | pmid = 17226784 | pmc = | doi = 10.1002/humu.20469 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: RDX radixin| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5962| accessdate = }}</ref>
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| update_protein_box = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
Radixin is a [[cytoskeletal]] protein that may be important in linking [[actin]] to the plasma membrane. It is highly similar in sequence to both [[ezrin]] and [[moesin]]. The radixin gene has been localized by fluorescence in situ hybridization to 11q23. A truncated version representing a [[pseudogene]] (RDXP2) was assigned to [[X chromosome|X]]p21.3. Another pseudogene that seemed to lack [[intron]]s (RDXP1) was mapped to 11p by Southern and PCR analyses.<ref name="entrez" />
{{GNF_Protein_box
| image = PBB_Protein_RDX_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1gc6.
| PDB = {{PDB2|1gc6}}, {{PDB2|1gc7}}, {{PDB2|1j19}}, {{PDB2|2d10}}, {{PDB2|2d11}}, {{PDB2|2d2q}}, {{PDB2|2yvc}}
| Name = Radixin
| HGNCid = 9944
| Symbol = RDX
| AltSymbols =;
| OMIM = 179410
| ECnumber = 
| Homologene = 37707
| MGIid = 97887
| GeneAtlas_image1 = PBB_GE_RDX_204969_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_RDX_212397_at_tn.png
| GeneAtlas_image3 = PBB_GE_RDX_212398_at_tn.png
| Function = {{GNF_GO|id=GO:0003779 |text = actin binding}} {{GNF_GO|id=GO:0005198 |text = structural molecule activity}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005902 |text = microvillus}} {{GNF_GO|id=GO:0015629 |text = actin cytoskeleton}}
| Process = {{GNF_GO|id=GO:0007016 |text = cytoskeletal anchoring}} {{GNF_GO|id=GO:0030033 |text = microvillus biogenesis}} {{GNF_GO|id=GO:0045176 |text = apical protein localization}} {{GNF_GO|id=GO:0051016 |text = barbed-end actin filament capping}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 5962
    | Hs_Ensembl = ENSG00000137710
    | Hs_RefseqProtein = NP_002897
    | Hs_RefseqmRNA = NM_002906
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 11
    | Hs_GenLoc_start = 109605378
    | Hs_GenLoc_end = 109672647
    | Hs_Uniprot = P35241
    | Mm_EntrezGene = 19684
    | Mm_Ensembl = ENSMUSG00000032050
    | Mm_RefseqmRNA = NM_009041
    | Mm_RefseqProtein = NP_033067
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 9
    | Mm_GenLoc_start = 51799393
    | Mm_GenLoc_end = 51841094
    | Mm_Uniprot = Q3TH46
  }}
}}
'''Radixin''', also known as '''RDX''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: RDX radixin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5962| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Interactions ==
{{PBB_Summary
| section_title =  
| summary_text = Radixin is a cytoskeletal protein that may be important in linking actin to the plasma membrane. It is highly similar in sequence to both ezrin and moesin. The radixin gene has been localized by fluorescence in situ hybridization to 11q23. A truncated version representing a pseudogene (RDXP2) was assigned to Xp21.3. Another pseudogene that seemed to lack introns (RDXP1) was mapped to 11p by Southern and PCR analyses.<ref name="entrez">{{cite web | title = Entrez Gene: RDX radixin| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5962| accessdate = }}</ref>
}}


==References==
Radixin has been shown to [[Protein-protein interaction|interact]] with [[GNA13]].<ref name=pmid10816569>{{cite journal | vauthors = Vaiskunaite R, Adarichev V, Furthmayr H, Kozasa T, Gudkov A, Voyno-Yasenetskaya TA | title = Conformational activation of radixin by G13 protein alpha subunit | journal = J. Biol. Chem. | volume = 275 | issue = 34 | pages = 26206–12 | date = August 2000 | pmid = 10816569 | doi = 10.1074/jbc.M001863200 }}</ref>
{{reflist|2}}
 
==Further reading==
== See also ==
* [[ERM protein family]]
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = Hoeflich KP, Ikura M | title = Radixin: cytoskeletal adopter and signaling protein | journal = Int. J. Biochem. Cell Biol. | volume = 36 | issue = 11 | pages = 2131–6 | year = 2005 | pmid = 15313460 | doi = 10.1016/j.biocel.2003.11.018 }}
| citations =
* {{cite journal | vauthors = Matarrese P, Malorni W | title = Human immunodeficiency virus (HIV)-1 proteins and cytoskeleton: partners in viral life and host cell death | journal = Cell Death Differ. | volume = 12 Suppl 1 | issue =  | pages = 932–41 | year = 2006 | pmid = 15818415 | doi = 10.1038/sj.cdd.4401582 }}
*{{cite journal | author=Hoeflich KP, Ikura M |title=Radixin: cytoskeletal adopter and signaling protein. |journal=Int. J. Biochem. Cell Biol. |volume=36 |issue= 11 |pages= 2131-6 |year= 2005 |pmid= 15313460 |doi= 10.1016/j.biocel.2003.11.018 }}
* {{cite journal | vauthors = Sato N, Funayama N, Nagafuchi A, Yonemura S, Tsukita S, Tsukita S | title = A gene family consisting of ezrin, radixin and moesin. Its specific localization at actin filament/plasma membrane association sites | journal = J. Cell Sci. | volume = 103 | issue = 1 | pages = 131–43 | year = 1992 | pmid = 1429901 | doi =  }}
*{{cite journal | author=Matarrese P, Malorni W |title=Human immunodeficiency virus (HIV)-1 proteins and cytoskeleton: partners in viral life and host cell death. |journal=Cell Death Differ. |volume=12 Suppl 1 |issue=  |pages= 932-41 |year= 2006 |pmid= 15818415 |doi= 10.1038/sj.cdd.4401582 }}
* {{cite journal | vauthors = Hirao M, Sato N, Kondo T, Yonemura S, Monden M, Sasaki T, Takai Y, Tsukita S, Tsukita S | title = Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway | journal = J. Cell Biol. | volume = 135 | issue = 1 | pages = 37–51 | year = 1996 | pmid = 8858161 | pmc = 2121020 | doi = 10.1083/jcb.135.1.37 }}
*{{cite journal | author=Sato N, Funayama N, Nagafuchi A, ''et al.'' |title=A gene family consisting of ezrin, radixin and moesin. Its specific localization at actin filament/plasma membrane association sites. |journal=J. Cell. Sci. |volume=103 ( Pt 1) |issue= |pages= 131-43 |year= 1992 |pmid= 1429901 |doi=  }}
* {{cite journal | vauthors = Bonaldo MF, Lennon G, Soares MB | title = Normalization and subtraction: two approaches to facilitate gene discovery | journal = Genome Res. | volume = 6 | issue = 9 | pages = 791–806 | year = 1997 | pmid = 8889548 | doi = 10.1101/gr.6.9.791 }}
*{{cite journal | author=Wilgenbus KK, Milatovich A, Francke U, Furthmayr H |title=Molecular cloning, cDNA sequence, and chromosomal assignment of the human radixin gene and two dispersed pseudogenes. |journal=Genomics |volume=16 |issue= 1 |pages= 199-206 |year= 1993 |pmid= 8486357 |doi= 10.1006/geno.1993.1159 }}
* {{cite journal | vauthors = Stemmer-Rachamimov AO, Gonzalez-Agosti C, Xu L, Burwick JA, Beauchamp R, Pinney D, Louis DN, Ramesh V | title = Expression of NF2-encoded merlin and related ERM family proteins in the human central nervous system | journal = J. Neuropathol. Exp. Neurol. | volume = 56 | issue = 6 | pages = 735–42 | year = 1997 | pmid = 9184664 | doi = 10.1097/00005072-199756060-00011 }}
*{{cite journal | author=Hirao M, Sato N, Kondo T, ''et al.'' |title=Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway. |journal=J. Cell Biol. |volume=135 |issue= 1 |pages= 37-51 |year= 1996 |pmid= 8858161 |doi= }}
* {{cite journal | vauthors = Takahashi K, Sasaki T, Mammoto A, Takaishi K, Kameyama T, Tsukita S, Takai Y | title = Direct interaction of the Rho GDP dissociation inhibitor with ezrin/radixin/moesin initiates the activation of the Rho small G protein | journal = J. Biol. Chem. | volume = 272 | issue = 37 | pages = 23371–5 | year = 1997 | pmid = 9287351 | doi = 10.1074/jbc.272.37.23371 }}
*{{cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
* {{cite journal | vauthors = Kondo T, Takeuchi K, Doi Y, Yonemura S, Nagata S, Tsukita S | title = ERM (Ezrin/Radixin/Moesin)-based Molecular Mechanism of Microvillar Breakdown at an Early Stage of Apoptosis | journal = J. Cell Biol. | volume = 139 | issue = 3 | pages = 749–58 | year = 1997 | pmid = 9348291 | pmc = 2141718 | doi = 10.1083/jcb.139.3.749 }}
*{{cite journal | author=Stemmer-Rachamimov AO, Gonzalez-Agosti C, Xu L, ''et al.'' |title=Expression of NF2-encoded merlin and related ERM family proteins in the human central nervous system. |journal=J. Neuropathol. Exp. Neurol. |volume=56 |issue= 6 |pages= 735-42 |year= 1997 |pmid= 9184664 |doi= }}
* {{cite journal | vauthors = Murthy A, Gonzalez-Agosti C, Cordero E, Pinney D, Candia C, Solomon F, Gusella J, Ramesh V | title = NHE-RF, a regulatory cofactor for Na(+)-H+ exchange, is a common interactor for merlin and ERM (MERM) proteins | journal = J. Biol. Chem. | volume = 273 | issue = 3 | pages = 1273–6 | year = 1998 | pmid = 9430655 | doi = 10.1074/jbc.273.3.1273 }}
*{{cite journal | author=Takahashi K, Sasaki T, Mammoto A, ''et al.'' |title=Direct interaction of the Rho GDP dissociation inhibitor with ezrin/radixin/moesin initiates the activation of the Rho small G protein. |journal=J. Biol. Chem. |volume=272 |issue= 37 |pages= 23371-5 |year= 1997 |pmid= 9287351 |doi= }}
* {{cite journal | vauthors = Matsui T, Maeda M, Doi Y, Yonemura S, Amano M, Kaibuchi K, Tsukita S, Tsukita S | title = Rho-Kinase Phosphorylates COOH-terminal Threonines of Ezrin/Radixin/Moesin (ERM) Proteins and Regulates Their Head-to-Tail Association | journal = J. Cell Biol. | volume = 140 | issue = 3 | pages = 647–57 | year = 1998 | pmid = 9456324 | pmc = 2140160 | doi = 10.1083/jcb.140.3.647 }}
*{{cite journal | author=Kondo T, Takeuchi K, Doi Y, ''et al.'' |title=ERM (ezrin/radixin/moesin)-based molecular mechanism of microvillar breakdown at an early stage of apoptosis. |journal=J. Cell Biol. |volume=139 |issue= 3 |pages= 749-58 |year= 1997 |pmid= 9348291 |doi= }}
* {{cite journal | vauthors = Yonemura S, Hirao M, Doi Y, Takahashi N, Kondo T, Tsukita S, Tsukita S | title = Ezrin/Radixin/Moesin (ERM) Proteins Bind to a Positively Charged Amino Acid Cluster in the Juxta-Membrane Cytoplasmic Domain of CD44, CD43, and ICAM-2 | journal = J. Cell Biol. | volume = 140 | issue = 4 | pages = 885–95 | year = 1998 | pmid = 9472040 | pmc = 2141743 | doi = 10.1083/jcb.140.4.885 }}
*{{cite journal | author=Murthy A, Gonzalez-Agosti C, Cordero E, ''et al.'' |title=NHE-RF, a regulatory cofactor for Na(+)-H+ exchange, is a common interactor for merlin and ERM (MERM) proteins. |journal=J. Biol. Chem. |volume=273 |issue= 3 |pages= 1273-6 |year= 1998 |pmid= 9430655 |doi= }}
* {{cite journal | vauthors = Bhartur SG, Goldenring JR | title = Mapping of ezrin dimerization using yeast two-hybrid screening | journal = Biochem. Biophys. Res. Commun. | volume = 243 | issue = 3 | pages = 874–7 | year = 1998 | pmid = 9501018 | doi = 10.1006/bbrc.1998.8196 }}
*{{cite journal | author=Matsui T, Maeda M, Doi Y, ''et al.'' |title=Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin (ERM) proteins and regulates their head-to-tail association. |journal=J. Cell Biol. |volume=140 |issue= 3 |pages= 647-57 |year= 1998 |pmid= 9456324 |doi= }}
* {{cite journal | vauthors = Takahashi K, Sasaki T, Mammoto A, Hotta I, Takaishi K, Imamura H, Nakano K, Kodama A, Takai Y | title = Interaction of radixin with Rho small G protein GDP/GTP exchange protein Dbl | journal = Oncogene | volume = 16 | issue = 25 | pages = 3279–84 | year = 1998 | pmid = 9681826 | doi = 10.1038/sj.onc.1201874 }}
*{{cite journal | author=Yonemura S, Hirao M, Doi Y, ''et al.'' |title=Ezrin/radixin/moesin (ERM) proteins bind to a positively charged amino acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and ICAM-2. |journal=J. Cell Biol. |volume=140 |issue= 4 |pages= 885-95 |year= 1998 |pmid= 9472040 |doi= }}
* {{cite journal | vauthors = Lamb RF, Roy C, Diefenbach TJ, Vinters HV, Johnson MW, Jay DG, Hall A | title = The TSC1 tumour suppressor hamartin regulates cell adhesion through ERM proteins and the GTPase Rho | journal = Nat. Cell Biol. | volume = 2 | issue = 5 | pages = 281–7 | year = 2000 | pmid = 10806479 | doi = 10.1038/35010550 }}
*{{cite journal | author=Bhartur SG, Goldenring JR |title=Mapping of ezrin dimerization using yeast two-hybrid screening. |journal=Biochem. Biophys. Res. Commun. |volume=243 |issue= 3 |pages= 874-7 |year= 1998 |pmid= 9501018 |doi= 10.1006/bbrc.1998.8196 }}
* {{cite journal | vauthors = Vaiskunaite R, Adarichev V, Furthmayr H, Kozasa T, Gudkov A, Voyno-Yasenetskaya TA | title = Conformational activation of radixin by G13 protein alpha subunit | journal = J. Biol. Chem. | volume = 275 | issue = 34 | pages = 26206–12 | year = 2000 | pmid = 10816569 | doi = 10.1074/jbc.M001863200 }}
*{{cite journal | author=Takahashi K, Sasaki T, Mammoto A, ''et al.'' |title=Interaction of radixin with Rho small G protein GDP/GTP exchange protein Dbl. |journal=Oncogene |volume=16 |issue= 25 |pages= 3279-84 |year= 1998 |pmid= 9681826 |doi= 10.1038/sj.onc.1201874 }}
* {{cite journal | vauthors = Hamada K, Shimizu T, Matsui T, Tsukita S, Tsukita S, Hakoshima T | title = Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tail of the adhesion protein ICAM-2 | journal = Acta Crystallogr. D | volume = 57 | issue = Pt 6 | pages = 891–2 | year = 2001 | pmid = 11375520 | doi = 10.1107/S0907444901005716 }}
*{{cite journal | author=Lamb RF, Roy C, Diefenbach TJ, ''et al.'' |title=The TSC1 tumour suppressor hamartin regulates cell adhesion through ERM proteins and the GTPase Rho. |journal=Nat. Cell Biol. |volume=2 |issue= 5 |pages= 281-7 |year= 2000 |pmid= 10806479 |doi= 10.1038/35010550 }}
* {{cite journal | vauthors = Kikuchi S, Hata M, Fukumoto K, Yamane Y, Matsui T, Tamura A, Yonemura S, Yamagishi H, Keppler D, Tsukita S, Tsukita S | title = Radixin deficiency causes conjugated hyperbilirubinemia with loss of Mrp2 from bile canalicular membranes | journal = Nat. Genet. | volume = 31 | issue = 3 | pages = 320–5 | year = 2002 | pmid = 12068294 | doi = 10.1038/ng905 }}
*{{cite journal | author=Vaiskunaite R, Adarichev V, Furthmayr H, ''et al.'' |title=Conformational activation of radixin by G13 protein alpha subunit. |journal=J. Biol. Chem. |volume=275 |issue= 34 |pages= 26206-12 |year= 2000 |pmid= 10816569 |doi= 10.1074/jbc.M001863200 }}
* {{cite journal | vauthors = Dickson TC, Mintz CD, Benson DL, Salton SR | title = Functional binding interaction identified between the axonal CAM L1 and members of the ERM family | journal = J. Cell Biol. | volume = 157 | issue = 7 | pages = 1105–12 | year = 2002 | pmid = 12070130 | pmc = 2173555 | doi = 10.1083/jcb.200111076 }}
*{{cite journal | author=Hamada K, Shimizu T, Matsui T, ''et al.'' |title=Crystallographic characterization of the radixin FERM domain bound to the cytoplasmic tail of the adhesion protein ICAM-2. |journal=Acta Crystallogr. D Biol. Crystallogr. |volume=57 |issue= Pt 6 |pages= 891-2 |year= 2001 |pmid= 11375520 |doi= }}
* {{cite journal | vauthors = Haddad LA, Smith N, Bowser M, Niida Y, Murthy V, Gonzalez-Agosti C, Ramesh V | title = The TSC1 tumor suppressor hamartin interacts with neurofilament-L and possibly functions as a novel integrator of the neuronal cytoskeleton | journal = J. Biol. Chem. | volume = 277 | issue = 46 | pages = 44180–6 | year = 2003 | pmid = 12226091 | doi = 10.1074/jbc.M207211200 }}
*{{cite journal | author=Kikuchi S, Hata M, Fukumoto K, ''et al.'' |title=Radixin deficiency causes conjugated hyperbilirubinemia with loss of Mrp2 from bile canalicular membranes. |journal=Nat. Genet. |volume=31 |issue= 3 |pages= 320-5 |year= 2002 |pmid= 12068294 |doi= 10.1038/ng905 }}
*{{cite journal | author=Dickson TC, Mintz CD, Benson DL, Salton SR |title=Functional binding interaction identified between the axonal CAM L1 and members of the ERM family. |journal=J. Cell Biol. |volume=157 |issue= 7 |pages= 1105-12 |year= 2002 |pmid= 12070130 |doi= 10.1083/jcb.200111076 }}
*{{cite journal  | author=Haddad LA, Smith N, Bowser M, ''et al.'' |title=The TSC1 tumor suppressor hamartin interacts with neurofilament-L and possibly functions as a novel integrator of the neuronal cytoskeleton. |journal=J. Biol. Chem. |volume=277 |issue= 46 |pages= 44180-6 |year= 2003 |pmid= 12226091 |doi= 10.1074/jbc.M207211200 }}
}}
{{refend}}
{{refend}}


{{protein-stub}}
{{PDB Gallery|geneid=5962}}
{{WikiDoc Sources}}
 
 
{{gene-11-stub}}

Latest revision as of 20:46, 8 November 2017

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

Radixin is a protein that in humans is encoded by the RDX gene.[1][2][3]

Radixin is a cytoskeletal protein that may be important in linking actin to the plasma membrane. It is highly similar in sequence to both ezrin and moesin. The radixin gene has been localized by fluorescence in situ hybridization to 11q23. A truncated version representing a pseudogene (RDXP2) was assigned to Xp21.3. Another pseudogene that seemed to lack introns (RDXP1) was mapped to 11p by Southern and PCR analyses.[3]

Interactions

Radixin has been shown to interact with GNA13.[4]

See also

References

  1. Wilgenbus KK, Milatovich A, Francke U, Furthmayr H (June 1993). "Molecular cloning, cDNA sequence, and chromosomal assignment of the human radixin gene and two dispersed pseudogenes". Genomics. 16 (1): 199–206. doi:10.1006/geno.1993.1159. PMID 8486357.
  2. Khan SY, Ahmed ZM, Shabbir MI, Kitajiri S, Kalsoom S, Tasneem S, Shayiq S, Ramesh A, Srisailpathy S, Khan SN, Smith RJ, Riazuddin S, Friedman TB, Riazuddin S (April 2007). "Mutations of the RDX gene cause nonsyndromic hearing loss at the DFNB24 locus". Hum Mutat. 28 (5): 417–23. doi:10.1002/humu.20469. PMID 17226784.
  3. 3.0 3.1 "Entrez Gene: RDX radixin".
  4. Vaiskunaite R, Adarichev V, Furthmayr H, Kozasa T, Gudkov A, Voyno-Yasenetskaya TA (August 2000). "Conformational activation of radixin by G13 protein alpha subunit". J. Biol. Chem. 275 (34): 26206–12. doi:10.1074/jbc.M001863200. PMID 10816569.

Further reading