ACTR3

ARP3 actin-related protein 3 homolog (yeast)
	; PDB rendering based on 1k8k.
Available structures
PDB	1k8k, 1tyq, 1u2v, 2p9i, 2p9k, 2p9l, 2p9n, 2p9p, 2p9s, 2p9u
Identifiers
Symbols	ACTR3; ARP3
External IDs	OMIM: 604222 MGI: 1921367 HomoloGene: 68483 GeneCards: ACTR3 Gene
Gene Ontology
Molecular function	• nucleotide binding; • actin binding; • protein binding; • ATP binding;
Cellular component	• Golgi membrane; • podosome; • cytoplasm; • actin filament; • Arp2/3 protein complex; • actin cytoskeleton; • lamellipodium; • hemidesmosome; • excitatory synapse;
Biological process	• cellular component movement; • response to carbohydrate stimulus; • positive regulation of lamellipodium assembly; • cell projection organization; • positive regulation of actin filament polymerization; • regulation of myosin II filament organization; • positive regulation of neuron differentiation; • response to antibiotic; • positive regulation of dendrite morphogenesis; • positive regulation of filopodium assembly; • response to protein stimulus; • cilium morphogenesis;
	Sources: Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs

From Wikipedia, the free encyclopedia

Jump to: navigation, search

Actin-related protein 3 is a protein that in humans is encoded by the ACTR3 gene.^[1]

The specific function of this gene has not yet been determined; however, the protein it encodes is known to be a major constituent of the ARP2/3 complex. This complex is located at the cell surface and is essential to cell shape and motility through lamellipodial actin assembly and protrusion.^[2]

[edit] Interactions

ACTR3 has been shown to interact with Cortactin.^[3]^[4]

[edit] References

^ Welch MD, DePace AH, Verma S, Iwamatsu A, Mitchison TJ (Aug 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2138188.
^ "Entrez Gene: ACTR3 ARP3 actin-related protein 3 homolog (yeast)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10096.
^ Weed, S A; Karginov A V, Schafer D A, Weaver A M, Kinley A W, Cooper J A, Parsons J T (Oct. 2000). "Cortactin localization to sites of actin assembly in lamellipodia requires interactions with F-actin and the Arp2/3 complex". J. Cell Biol. (UNITED STATES) 151 (1): 29–40. doi:10.1083/jcb.151.1.29. ISSN 0021-9525. PMC 2189811. PMID 11018051. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2189811.
^ Di Ciano, Caterina; Nie Zilin, Szászi Katalin, Lewis Alison, Uruno Takehito, Zhan Xi, Rotstein Ori D, Mak Alan, Kapus András (Sep. 2002). "Osmotic stress-induced remodeling of the cortical cytoskeleton". Am. J. Physiol., Cell Physiol. (United States) 283 (3): C850–65. doi:10.1152/ajpcell.00018.2002. ISSN 0363-6143. PMID 12176742.

[edit] 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.
Winter D, Podtelejnikov AV, Mann M, Li R (1997). "The complex containing actin-related proteins Arp2 and Arp3 is required for the motility and integrity of yeast actin patches". Curr. Biol. 7 (7): 519–29. doi:10.1016/S0960-9822(06)00223-5. PMID 9210376.
Machesky LM, Reeves E, Wientjes F et al (1998). "Mammalian actin-related protein 2/3 complex localizes to regions of lamellipodial protrusion and is composed of evolutionarily conserved proteins". Biochem. J. 328 (1): 105–12. PMC 1218893. PMID 9359840. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1218893.
Ma L, Rohatgi R, Kirschner MW (1999). "The Arp2/3 complex mediates actin polymerization induced by the small GTP-binding protein Cdc42". Proc. Natl. Acad. Sci. U.S.A. 95 (26): 15362–7. doi:10.1073/pnas.95.26.15362. PMC 28048. PMID 9860974. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=28048.
Machesky LM, Insall RH (1999). "Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex". Curr. Biol. 8 (25): 1347–56. doi:10.1016/S0960-9822(98)00015-3. PMID 9889097.
Suetsugu S, Miki H, Takenawa T (1999). "Identification of two human WAVE/SCAR homologues as general actin regulatory molecules which associate with the Arp2/3 complex". Biochem. Biophys. Res. Commun. 260 (1): 296–302. doi:10.1006/bbrc.1999.0894. PMID 10381382.
May RC, Hall ME, Higgs HN et al (1999). "The Arp2/3 complex is essential for the actin-based motility of Listeria monocytogenes". Curr. Biol. 9 (14): 759–62. doi:10.1016/S0960-9822(99)80337-6. PMID 10421578.
Loisel TP, Boujemaa R, Pantaloni D, Carlier MF (1999). "Reconstitution of actin-based motility of Listeria and Shigella using pure proteins". Nature 401 (6753): 613–6. doi:10.1038/44183. PMID 10524632.
Higgs HN, Blanchoin L, Pollard TD (1999). "Influence of the C terminus of Wiskott-Aldrich syndrome protein (WASp) and the Arp2/3 complex on actin polymerization". Biochemistry 38 (46): 15212–22. doi:10.1021/bi991843. PMID 10563804.
Carlier MF, Nioche P, Broutin-L'Hermite I et al (2000). "GRB2 links signaling to actin assembly by enhancing interaction of neural Wiskott-Aldrich syndrome protein (N-WASp) with actin-related protein (ARP2/3) complex". J. Biol. Chem. 275 (29): 21946–52. doi:10.1074/jbc.M000687200. PMID 10781580.
Jay P, Bergé-Lefranc JL, Massacrier A et al (2000). "ARP3beta, the gene encoding a new human actin-related protein, is alternatively spliced and predominantly expressed in brain neuronal cells". Eur. J. Biochem. 267 (10): 2921–8. doi:10.1046/j.1432-1327.2000.01306.x. PMID 10806390.
Weed SA, Karginov AV, Schafer DA et al (2000). "Cortactin localization to sites of actin assembly in lamellipodia requires interactions with F-actin and the Arp2/3 complex". J. Cell Biol. 151 (1): 29–40. doi:10.1083/jcb.151.1.29. PMC 2189811. PMID 11018051. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2189811.
Prehoda KE, Scott JA, Mullins RD, Lim WA (2000). "Integration of multiple signals through cooperative regulation of the N-WASP-Arp2/3 complex". Science 290 (5492): 801–6. doi:10.1126/science.290.5492.801. PMID 11052943.
Marchand JB, Kaiser DA, Pollard TD, Higgs HN (2001). "Interaction of WASP/Scar proteins with actin and vertebrate Arp2/3 complex". Nat. Cell Biol. 3 (1): 76–82. doi:10.1038/35050590. PMID 11146629.
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 et al (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 et al (2002). "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.
Andersen JS, Lyon CE, Fox AH et al (2002). "Directed proteomic analysis of the human nucleolus". Curr. Biol. 12 (1): 1–11. doi:10.1016/S0960-9822(01)00650-9. PMID 11790298.
Kovacs EM, Goodwin M, Ali RG et al (2002). "Cadherin-directed actin assembly: E-cadherin physically associates with the Arp2/3 complex to direct actin assembly in nascent adhesive contacts". Curr. Biol. 12 (5): 379–82. doi:10.1016/S0960-9822(02)00661-9. PMID 11882288.