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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''Actin-related protein 2/3 complex subunit 4''' is a [[protein]] that in humans is encoded by the ''ARPC4'' [[gene]].<ref name="pmid9230079">{{cite journal | vauthors = Welch MD, DePace AH, Verma S, Iwamatsu A, Mitchison TJ | title = The human Arp2/3 complex is composed of evolutionarily conserved subunits and is localized to cellular regions of dynamic actin filament assembly | journal = J. Cell Biol. | volume = 138 | issue = 2 | pages = 375–84  | date = August 1997 | pmid = 9230079 | pmc = 2138188 | doi = 10.1083/jcb.138.2.375 }}</ref><ref name="pmid9359840">{{cite journal | vauthors = Machesky LM, Reeves E, Wientjes F, Mattheyse FJ, Grogan A, Totty NF, Burlingame AL, Hsuan JJ, Segal AW | title = Mammalian actin-related protein 2/3 complex localizes to regions of lamellipodial protrusion and is composed of evolutionarily conserved proteins | journal = Biochem. J. | volume = 328 ( Pt 1) | issue = 1 | pages = 105–12 | year = 1997 | date = January 1998 | pmid = 9359840 | pmc = 1218893 | doi =  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: ARPC4 actin related protein 2/3 complex, subunit 4, 20kDa| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10093| accessdate = }}</ref>
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_ARPC4_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1k8k.
| PDB = {{PDB2|1k8k}}, {{PDB2|1tyq}}, {{PDB2|1u2v}}, {{PDB2|2p9i}}, {{PDB2|2p9k}}, {{PDB2|2p9l}}, {{PDB2|2p9n}}, {{PDB2|2p9p}}, {{PDB2|2p9s}}, {{PDB2|2p9u}}
| Name = Actin related protein 2/3 complex, subunit 4, 20kDa
| HGNCid = 707
| Symbol = ARPC4
| AltSymbols =; ARC20; MGC13544; p20-Arc
| OMIM = 604226
| ECnumber = 
| Homologene = 4177
| MGIid = 1915339
| Function = {{GNF_GO|id=GO:0005200 |text = structural constituent of cytoskeleton}} {{GNF_GO|id=GO:0030674 |text = protein binding, bridging}} {{GNF_GO|id=GO:0051015 |text = actin filament binding}}
| Component = {{GNF_GO|id=GO:0005856 |text = cytoskeleton}} {{GNF_GO|id=GO:0005885 |text = Arp2/3 protein complex}}
| Process = {{GNF_GO|id=GO:0030041 |text = actin filament polymerization}} {{GNF_GO|id=GO:0045010 |text = actin nucleation}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 10093
    | Hs_Ensembl = 
    | Hs_RefseqProtein = NP_001020130
    | Hs_RefseqmRNA = NM_001024959
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 
    | Hs_GenLoc_start = 
    | Hs_GenLoc_end = 
    | Hs_Uniprot = 
    | Mm_EntrezGene = 68089
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = NM_026552
    | Mm_RefseqProtein = NP_080828
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot = 
  }}
}}
'''Actin related protein 2/3 complex, subunit 4, 20kDa''', also known as '''ARPC4''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ARPC4 actin related protein 2/3 complex, subunit 4, 20kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10093| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
This gene encodes one of seven subunits of the human Arp2/3 protein complex. The Arp2/3 protein complex has been implicated in the control of actin polymerization in cells and has been conserved through evolution. The exact role of the protein encoded by this gene, the p20 subunit, has yet to be determined. Three transcript variants encoding two distinct isoforms have been found for this gene.<ref name="entrez"/>
{{PBB_Summary
| section_title =
| summary_text = This gene encodes one of seven subunits of the human Arp2/3 protein complex. The Arp2/3 protein complex has been implicated in the control of actin polymerization in cells and has been conserved through evolution. The exact role of the protein encoded by this gene, the p20 subunit, has yet to be determined. Three transcript variants encoding two distinct isoforms have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: ARPC4 actin related protein 2/3 complex, subunit 4, 20kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10093| accessdate = }}</ref>
}}


==References==
==Model organisms==
{{reflist|2}}
{| class="wikitable sortable collapsible collapsed" border="1" cellpadding="2" style="float: right;" |
==Further reading==
|+ ''Arpc4'' knockout mouse phenotype
{{refbegin | 2}}
|-
{{PBB_Further_reading
! Characteristic!! Phenotype
| citations =
*{{cite journal  | author=Welch MD, Iwamatsu A, Mitchison TJ |title=Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes. |journal=Nature |volume=385 |issue= 6613 |pages= 265-9 |year= 1997 |pmid= 9000076 |doi= 10.1038/385265a0 }}
*{{cite journal  | author=Welch MD, DePace AH, Verma S, ''et al.'' |title=The human Arp2/3 complex is composed of evolutionarily conserved subunits and is localized to cellular regions of dynamic actin filament assembly. |journal=J. Cell Biol. |volume=138 |issue= 2 |pages= 375-84 |year= 1997 |pmid= 9230079 |doi=  }}
*{{cite journal  | author=Machesky LM, Reeves E, Wientjes F, ''et al.'' |title=Mammalian actin-related protein 2/3 complex localizes to regions of lamellipodial protrusion and is composed of evolutionarily conserved proteins. |journal=Biochem. J. |volume=328 ( Pt 1) |issue=  |pages= 105-12 |year= 1998 |pmid= 9359840 |doi=  }}
*{{cite journal  | author=Zhao X, Yang Z, Qian M, Zhu X |title=Interactions among subunits of human Arp2/3 complex: p20-Arc as the hub. |journal=Biochem. Biophys. Res. Commun. |volume=280 |issue= 2 |pages= 513-7 |year= 2001 |pmid= 11162547 |doi= 10.1006/bbrc.2000.4151 }}
*{{cite journal  | author=Robinson RC, Turbedsky K, Kaiser DA, ''et al.'' |title=Crystal structure of Arp2/3 complex. |journal=Science |volume=294 |issue= 5547 |pages= 1679-84 |year= 2001 |pmid= 11721045 |doi= 10.1126/science.1066333 }}
*{{cite journal  | author=Gournier H, Goley ED, Niederstrasser H, ''et al.'' |title=Reconstitution of human Arp2/3 complex reveals critical roles of individual subunits in complex structure and activity. |journal=Mol. Cell |volume=8 |issue= 5 |pages= 1041-52 |year= 2002 |pmid= 11741539 |doi=  }}
*{{cite journal  | author=Millard TH, Behrendt B, Launay S, ''et al.'' |title=Identification and characterisation of a novel human isoform of Arp2/3 complex subunit p16-ARC/ARPC5. |journal=Cell Motil. Cytoskeleton |volume=54 |issue= 1 |pages= 81-90 |year= 2003 |pmid= 12451597 |doi= 10.1002/cm.10087 }}
*{{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  | author=Gevaert K, Goethals M, Martens L, ''et al.'' |title=Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. |journal=Nat. Biotechnol. |volume=21 |issue= 5 |pages= 566-9 |year= 2004 |pmid= 12665801 |doi= 10.1038/nbt810 }}
*{{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  | 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  | author=Andersen JS, Lam YW, Leung AK, ''et al.'' |title=Nucleolar proteome dynamics. |journal=Nature |volume=433 |issue= 7021 |pages= 77-83 |year= 2005 |pmid= 15635413 |doi= 10.1038/nature03207 }}
*{{cite journal  | author=Stelzl U, Worm U, Lalowski M, ''et al.'' |title=A human protein-protein interaction network: a resource for annotating the proteome. |journal=Cell |volume=122 |issue= 6 |pages= 957-68 |year= 2005 |pmid= 16169070 |doi= 10.1016/j.cell.2005.08.029 }}
*{{cite journal  | author=Rosentreter A, Hofmann A, Xavier CP, ''et al.'' |title=Coronin 3 involvement in F-actin-dependent processes at the cell cortex. |journal=Exp. Cell Res. |volume=313 |issue= 5 |pages= 878-95 |year= 2007 |pmid= 17274980 |doi= 10.1016/j.yexcr.2006.12.015 }}
*{{cite journal  | author=Ewing RM, Chu P, Elisma F, ''et al.'' |title=Large-scale mapping of human protein-protein interactions by mass spectrometry. |journal=Mol. Syst. Biol. |volume=3 |issue=  |pages= 89 |year= 2007 |pmid= 17353931 |doi= 10.1038/msb4100134 }}
}}
{{refend}}


{{protein-stub}}
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| [[Homozygote]] viability || bgcolor="#C40000"|Abnormal
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| [[Open Field (animal test)|Anxiety]] || bgcolor="#488ED3"|Normal
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| Grip strength || bgcolor="#488ED3"|Normal
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| [[Hot plate test|Hot plate]] || bgcolor="#488ED3"|Normal
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| [[Dysmorphology]] || bgcolor="#488ED3"|Normal<ref name="Dysmorphology">{{cite web |url=http://www.sanger.ac.uk/mouseportal/phenotyping/MALT/dysmorphology/ |title=Dysmorphology data for Arpc4 |publisher=Wellcome Trust Sanger Institute}}</ref>
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| [[Indirect calorimetry]] || bgcolor="#488ED3"|Normal
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| [[Glucose tolerance test]] || bgcolor="#488ED3"|Normal
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| [[Auditory brainstem response]] || bgcolor="#488ED3"|Normal
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| [[Dual-energy X-ray absorptiometry|DEXA]] || bgcolor="#488ED3"|Normal
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| [[Radiography]] || bgcolor="#488ED3"|Normal
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| Body temperature || bgcolor="#488ED3"|Normal
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| Eye morphology || bgcolor="#488ED3"|Normal
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| [[Clinical chemistry]] || bgcolor="#488ED3"|Normal
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| [[Blood plasma|Plasma]] [[immunoglobulin]]s || bgcolor="#488ED3"|Normal
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| [[Haematology]] || bgcolor="#488ED3"|Normal
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| [[Peripheral blood lymphocyte]]s || bgcolor="#488ED3"|Normal
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| [[Micronucleus test]] || bgcolor="#488ED3"|Normal
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| Heart weight || bgcolor="#488ED3"|Normal
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| Brain histopathology || bgcolor="#488ED3"|Normal
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| Eye Histopathology || bgcolor="#488ED3"|Normal
|-
| ''[[Salmonella]]'' infection || bgcolor="#488ED3"|Normal<ref name="''Salmonella'' infection">{{cite web |url=http://www.sanger.ac.uk/mouseportal/phenotyping/MALT/salmonella-challenge/ |title=''Salmonella'' infection data for Arpc4 |publisher=Wellcome Trust Sanger Institute}}</ref>
|-
| ''[[Citrobacter]]'' infection || bgcolor="#488ED3"|Normal<ref name="''Citrobacter'' infection">{{cite web |url=http://www.sanger.ac.uk/mouseportal/phenotyping/MALT/citrobacter-challenge/ |title=''Citrobacter'' infection data for Arpc4 |publisher=Wellcome Trust Sanger Institute}}</ref>
|-
| colspan=2; style="text-align: center;" | All tests and analysis from<ref name="mgp_reference">{{cite journal | doi = 10.1111/j.1755-3768.2010.4142.x | title = The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice | year = 2010 | author = Gerdin AK | journal = Acta Ophthalmologica | volume = 88 | pages =  925–7 }}</ref><ref>[http://www.sanger.ac.uk/mouseportal/ Mouse Resources Portal], Wellcome Trust Sanger Institute.</ref>
|}
[[Model organism]]s have been used in the study of ARPC4 function. A conditional [[knockout mouse]] line, called ''Arpc4<sup>tm1a(EUCOMM)Wtsi</sup>''<ref name="allele_ref">{{cite web |url=http://www.knockoutmouse.org/martsearch/search?query=Arpc4 |title=International Knockout Mouse Consortium}}</ref><ref name="mgi_allele_ref">{{cite web |url=http://www.informatics.jax.org/searchtool/Search.do?query=MGI:4433308 |title=Mouse Genome Informatics}}</ref> was generated as part of the [[International Knockout Mouse Consortium]] program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.<ref name="pmid21677750">{{cite journal | vauthors = Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A | title = A conditional knockout resource for the genome-wide study of mouse gene function | journal = Nature | volume = 474 | issue = 7351 | pages = 337–42 | year = 2011 | pmid = 21677750 | pmc = 3572410 | doi = 10.1038/nature10163 }}</ref><ref name="mouse_library">{{cite journal | vauthors = Dolgin E | title = Mouse library set to be knockout | journal = Nature | volume = 474 | issue = 7351 | pages = 262–3 | year = 2011 | pmid = 21677718 | doi = 10.1038/474262a }}</ref><ref name="mouse_for_all_reasons">{{cite journal | vauthors = Collins FS, Rossant J, Wurst W | title = A mouse for all reasons | journal = Cell | volume = 128 | issue = 1 | pages = 9–13 | year = 2007 | pmid = 17218247 | doi = 10.1016/j.cell.2006.12.018 }}</ref>
 
Male and female animals underwent a standardized [[phenotypic screen]] to determine the effects of deletion.<ref name="mgp_reference" /><ref name="pmid21722353">{{cite journal | vauthors = van der Weyden L, White JK, Adams DJ, Logan DW | title = The mouse genetics toolkit: revealing function and mechanism | journal = Genome Biol. | volume = 12 | issue = 6 | pages = 224 | year = 2011 | pmid = 21722353 | pmc = 3218837 | doi = 10.1186/gb-2011-12-6-224 }}</ref> Twenty six tests were carried out on [[mutant]] mice and two significant abnormalities were observed.<ref name="mgp_reference" />  No [[homozygous]] [[mutant]] embryos were identified during gestation, and therefore none survived until [[weaning]]. The remaining tests were carried out on [[heterozygous]] mutant adult mice; no additional significant abnormalities were observed in these animals.<ref name="mgp_reference" />
 
== Interactions ==
 
ARPC4 has been shown to [[Protein-protein interaction|interact]] with [[ARPC5]].<ref name="pmid12451597">{{cite journal | vauthors = Millard TH, Behrendt B, Launay S, Fütterer K, Machesky LM | title = Identification and characterisation of a novel human isoform of Arp2/3 complex subunit p16-ARC/ARPC5 | journal = Cell Motil. Cytoskeleton | volume = 54 | issue = 1 | pages = 81–90 | year = 2003 | pmid = 12451597 | doi = 10.1002/cm.10087 }}</ref><ref name="pmid11162547">{{cite journal | vauthors = Zhao X, Yang Z, Qian M, Zhu X | title = Interactions among subunits of human Arp2/3 complex: p20-Arc as the hub | journal = Biochem. Biophys. Res. Commun. | volume = 280 | issue = 2 | pages = 513–7 | year = 2001 | pmid = 11162547 | doi = 10.1006/bbrc.2000.4151 }}</ref>
 
== References ==
{{Reflist}}
 
== Further reading ==
{{Refbegin | 2}}
* {{cite journal | vauthors = Welch MD, Iwamatsu A, Mitchison TJ | title = Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes | journal = Nature | volume = 385 | issue = 6613 | pages = 265–9 | year = 1997 | pmid = 9000076 | doi = 10.1038/385265a0 }}
* {{cite journal | vauthors = Zhao X, Yang Z, Qian M, Zhu X | title = Interactions among subunits of human Arp2/3 complex: p20-Arc as the hub | journal = Biochem. Biophys. Res. Commun. | volume = 280 | issue = 2 | pages = 513–7 | year = 2001 | pmid = 11162547 | doi = 10.1006/bbrc.2000.4151 }}
* {{cite journal | vauthors = Robinson RC, Turbedsky K, Kaiser DA, Marchand JB, Higgs HN, Choe S, Pollard TD | title = Crystal structure of Arp2/3 complex | journal = Science | volume = 294 | issue = 5547 | pages = 1679–84 | year = 2001 | pmid = 11721045 | doi = 10.1126/science.1066333 }}
* {{cite journal | vauthors = Gournier H, Goley ED, Niederstrasser H, Trinh T, Welch MD | title = Reconstitution of human Arp2/3 complex reveals critical roles of individual subunits in complex structure and activity | journal = Mol. Cell | volume = 8 | issue = 5 | pages = 1041–52 | year = 2001 | pmid = 11741539 | doi = 10.1016/S1097-2765(01)00393-8 }}
* {{cite journal | vauthors = Millard TH, Behrendt B, Launay S, Fütterer K, Machesky LM | title = Identification and characterisation of a novel human isoform of Arp2/3 complex subunit p16-ARC/ARPC5 | journal = Cell Motil. Cytoskeleton | volume = 54 | issue = 1 | pages = 81–90 | year = 2003 | pmid = 12451597 | doi = 10.1002/cm.10087 }}
* {{cite journal | vauthors = Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J | title = Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides | journal = Nat. Biotechnol. | volume = 21 | issue = 5 | pages = 566–9 | year = 2003 | pmid = 12665801 | doi = 10.1038/nbt810 }}
* {{cite journal | vauthors = Andersen JS, Lam YW, Leung AK, Ong SE, Lyon CE, Lamond AI, Mann M | title = Nucleolar proteome dynamics | journal = Nature | volume = 433 | issue = 7021 | pages = 77–83 | year = 2005 | pmid = 15635413 | doi = 10.1038/nature03207 }}
* {{cite journal | vauthors = Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE | title = A human protein-protein interaction network: a resource for annotating the proteome | journal = Cell | volume = 122 | issue = 6 | pages = 957–68 | year = 2005 | pmid = 16169070 | doi = 10.1016/j.cell.2005.08.029 }}
* {{cite journal | vauthors = Rosentreter A, Hofmann A, Xavier CP, Stumpf M, Noegel AA, Clemen CS | title = Coronin 3 involvement in F-actin-dependent processes at the cell cortex | journal = Exp. Cell Res. | volume = 313 | issue = 5 | pages = 878–95 | year = 2007 | pmid = 17274980 | doi = 10.1016/j.yexcr.2006.12.015 }}
* {{cite journal | vauthors = Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D | title = Large-scale mapping of human protein-protein interactions by mass spectrometry | journal = Mol. Syst. Biol. | volume = 3 | issue = 1 | pages = 89 | year = 2007 | pmid = 17353931 | pmc = 1847948 | doi = 10.1038/msb4100134 }}
{{Refend}}
 
== External links ==
* {{UCSC gene details|ARPC4}}
 
{{PDB Gallery|geneid=10093}}
 
[[Category:Genes mutated in mice]]

Revision as of 18:17, 29 August 2017

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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

Actin-related protein 2/3 complex subunit 4 is a protein that in humans is encoded by the ARPC4 gene.[1][2][3]

Function

This gene encodes one of seven subunits of the human Arp2/3 protein complex. The Arp2/3 protein complex has been implicated in the control of actin polymerization in cells and has been conserved through evolution. The exact role of the protein encoded by this gene, the p20 subunit, has yet to be determined. Three transcript variants encoding two distinct isoforms have been found for this gene.[3]

Model organisms

Model organisms have been used in the study of ARPC4 function. A conditional knockout mouse line, called Arpc4tm1a(EUCOMM)Wtsi[9][10] was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists.[11][12][13]

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[7][14] Twenty six tests were carried out on mutant mice and two significant abnormalities were observed.[7] No homozygous mutant embryos were identified during gestation, and therefore none survived until weaning. The remaining tests were carried out on heterozygous mutant adult mice; no additional significant abnormalities were observed in these animals.[7]

Interactions

ARPC4 has been shown to interact with ARPC5.[15][16]

References

  1. Welch MD, DePace AH, Verma S, Iwamatsu A, Mitchison TJ (August 1997). "The human Arp2/3 complex is composed of evolutionarily conserved subunits and is localized to cellular regions of dynamic actin filament assembly". J. Cell Biol. 138 (2): 375–84. doi:10.1083/jcb.138.2.375. PMC 2138188. PMID 9230079.
  2. Machesky LM, Reeves E, Wientjes F, Mattheyse FJ, Grogan A, Totty NF, Burlingame AL, Hsuan JJ, Segal AW (January 1998). "Mammalian actin-related protein 2/3 complex localizes to regions of lamellipodial protrusion and is composed of evolutionarily conserved proteins". Biochem. J. 328 ( Pt 1) (1): 105–12. PMC 1218893. PMID 9359840. Check date values in: |year= / |date= mismatch (help)
  3. 3.0 3.1 "Entrez Gene: ARPC4 actin related protein 2/3 complex, subunit 4, 20kDa".
  4. "Dysmorphology data for Arpc4". Wellcome Trust Sanger Institute.
  5. "Salmonella infection data for Arpc4". Wellcome Trust Sanger Institute.
  6. "Citrobacter infection data for Arpc4". Wellcome Trust Sanger Institute.
  7. 7.0 7.1 7.2 7.3 Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica. 88: 925–7. doi:10.1111/j.1755-3768.2010.4142.x.
  8. Mouse Resources Portal, Wellcome Trust Sanger Institute.
  9. "International Knockout Mouse Consortium".
  10. "Mouse Genome Informatics".
  11. Skarnes WC, Rosen B, West AP, Koutsourakis M, Bushell W, Iyer V, Mujica AO, Thomas M, Harrow J, Cox T, Jackson D, Severin J, Biggs P, Fu J, Nefedov M, de Jong PJ, Stewart AF, Bradley A (2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–42. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
  12. Dolgin E (2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
  13. Collins FS, Rossant J, Wurst W (2007). "A mouse for all reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
  14. van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism". Genome Biol. 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.
  15. Millard TH, Behrendt B, Launay S, Fütterer K, Machesky LM (2003). "Identification and characterisation of a novel human isoform of Arp2/3 complex subunit p16-ARC/ARPC5". Cell Motil. Cytoskeleton. 54 (1): 81–90. doi:10.1002/cm.10087. PMID 12451597.
  16. Zhao X, Yang Z, Qian M, Zhu X (2001). "Interactions among subunits of human Arp2/3 complex: p20-Arc as the hub". Biochem. Biophys. Res. Commun. 280 (2): 513–7. doi:10.1006/bbrc.2000.4151. PMID 11162547.

Further reading

  • Welch MD, Iwamatsu A, Mitchison TJ (1997). "Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes". Nature. 385 (6613): 265–9. doi:10.1038/385265a0. PMID 9000076.
  • Zhao X, Yang Z, Qian M, Zhu X (2001). "Interactions among subunits of human Arp2/3 complex: p20-Arc as the hub". Biochem. Biophys. Res. Commun. 280 (2): 513–7. doi:10.1006/bbrc.2000.4151. PMID 11162547.
  • Robinson RC, Turbedsky K, Kaiser DA, Marchand JB, Higgs HN, Choe S, Pollard TD (2001). "Crystal structure of Arp2/3 complex". Science. 294 (5547): 1679–84. doi:10.1126/science.1066333. PMID 11721045.
  • Gournier H, Goley ED, Niederstrasser H, Trinh T, Welch MD (2001). "Reconstitution of human Arp2/3 complex reveals critical roles of individual subunits in complex structure and activity". Mol. Cell. 8 (5): 1041–52. doi:10.1016/S1097-2765(01)00393-8. PMID 11741539.
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