ARPC4

ARPC4
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2P9N, 1TYQ, 1U2V, 4JD2, 3DXK, 3UKU, 3UKR, 2P9P, 2P9K, 2P9U, 3ULE, 3RSE, 2P9S, 2P9I, 4XF2, 2P9L, 1K8K, 3DXM, 4XEI
Identifiers
Aliases	ARPC4 , ARC20, P20-ARC, actin related protein 2/3 complex subunit 4
External IDs	OMIM: 604226 MGI: 1915339 HomoloGene: 4177 GeneCards: ARPC4
Gene location (Human) Chr. Chromosome 3 (human) [1] Band 3p25.3 Start 9,792,495 bp [1] End 9,807,101 bp [1]
Gene location (Mouse) Chr. Chromosome 6 (mouse) [2] Band 6|6 E3 Start 113,355,076 bp [2] End 113,367,409 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in monocyte rectum smooth muscle tissue right coronary artery gallbladder islet of Langerhans ascending aorta left coronary artery blood stromal cell of endometrium Top expressed in lip superior frontal gyrus thymus morula esophagus yolk sac duodenum somite placenta cerebellar cortex More reference expression data BioGPS n/a
Gene ontology Molecular function enzyme binding protein-macromolecule adaptor activity actin filament binding actin binding structural constituent of cytoskeleton protein binding Cellular component cytoplasm cytosol Arp2/3 protein complex cell projection extracellular exosome cytoskeleton actin cytoskeleton nucleus site of double-strand break Biological process ephrin receptor signaling pathway actin filament polymerization actin nucleation Fc-gamma receptor signaling pathway involved in phagocytosis Arp2/3 complex-mediated actin nucleation membrane organization regulation of actin filament polymerization Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 10093 68089 Ensembl ENSG00000241553 ENSMUSG00000079426 UniProt P59998 P59999 RefSeq (mRNA) NM_005718 NM_001024959 NM_001024960 NM_001198780 NM_001170485 NM_001170486 NM_026552 RefSeq (protein) NP_001020130 NP_001020131 NP_001185709 NP_005709 NP_001163956 NP_001163957 NP_080828 Location (UCSC) Chr 3: 9.79 – 9.81 Mb Chr 6: 113.36 – 113.37 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Actin-related protein 2/3 complex subunit 4 is a protein that in humans is encoded by the ARPC4 gene. ^{[5] [6] [7]}

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. ^[7]

Model organisms

Arpc4 knockout mouse phenotype

Characteristic	Phenotype
Homozygote viability	Abnormal
Recessive lethal study	Abnormal
Fertility	Normal
Body weight	Normal
Anxiety	Normal
Neurological assessment	Normal
Grip strength	Normal
Hot plate	Normal
Dysmorphology	Normal [8]
Indirect calorimetry	Normal
Glucose tolerance test	Normal
Auditory brainstem response	Normal
DEXA	Normal
Radiography	Normal
Body temperature	Normal
Eye morphology	Normal
Clinical chemistry	Normal
Plasma immunoglobulins	Normal
Haematology	Normal
Peripheral blood lymphocytes	Normal
Micronucleus test	Normal
Heart weight	Normal
Brain histopathology	Normal
Eye Histopathology	Normal
Salmonella infection	Normal [9]
Citrobacter infection	Normal [10]
All tests and analysis from [11] [12]

Model organisms have been used in the study of ARPC4 function. A conditional knockout mouse line, called Arpc4^{tm1a(EUCOMM)Wtsi [13] [14]} 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. ^{[15] [16] [17]}

Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion. ^{[11] [18]} Twenty six tests were carried out on mutant mice and two significant abnormalities were observed. ^[11] 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. ^[11]

Interactions

ARPC4 has been shown to interact with ARPC5. ^{[19] [20]}

References

1. GRCh38: Ensembl release 89: ENSG00000241553 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000079426 - 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. 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.
6. Machesky LM, Reeves E, Wientjes F, Mattheyse FJ, Grogan A, Totty NF, Burlingame AL, Hsuan JJ, Segal AW (1997). "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. doi:10.1042/bj3280105. PMC   1218893 . PMID   9359840.
7. "Entrez Gene: ARPC4 actin related protein 2/3 complex, subunit 4, 20kDa".
8. "Dysmorphology data for Arpc4". Wellcome Trust Sanger Institute.
9. "Salmonella infection data for Arpc4". Wellcome Trust Sanger Institute.
10. "Citrobacter infection data for Arpc4". Wellcome Trust Sanger Institute.
11. 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. S2CID   85911512.
12. Mouse Resources Portal, Wellcome Trust Sanger Institute.
13. "International Knockout Mouse Consortium".
14. "Mouse Genome Informatics".
15. 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.
16. Dolgin E (2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID   21677718.
17. 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. S2CID   18872015.
18. 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.
19. 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.
20. 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. Bibcode:1997Natur.385..265W. doi:10.1038/385265a0. PMID   9000076. S2CID   4358529.
• 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. Bibcode:2001Sci...294.1679R. doi:10.1126/science.1066333. PMID   11721045. S2CID   18088124.
• 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.
• Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J (2003). "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID   12665801. S2CID   23783563.
• Andersen JS, Lam YW, Leung AK, Ong SE, Lyon CE, Lamond AI, Mann M (2005). "Nucleolar proteome dynamics". Nature. 433 (7021): 77–83. Bibcode:2005Natur.433...77A. doi:10.1038/nature03207. PMID   15635413. S2CID   4344740.
• 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 (2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. hdl: 11858/00-001M-0000-0010-8592-0 . PMID   16169070. S2CID   8235923.
• Rosentreter A, Hofmann A, Xavier CP, Stumpf M, Noegel AA, Clemen CS (2007). "Coronin 3 involvement in F-actin-dependent processes at the cell cortex". Exp. Cell Res. 313 (5): 878–95. doi:10.1016/j.yexcr.2006.12.015. hdl: 10072/14982 . PMID   17274980.
• 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 (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC   1847948 . PMID   17353931.

External links

• ARPC4 human gene details in the UCSC Genome Browser .