ACTR3

From Wikipedia, the free encyclopedia

ARP3 actin-related protein 3 homolog (yeast)

PDB rendering based on 1k8k.

Available structures: 1k8k, 1tyq, 1u2v, 2p9i, 2p9k, 2p9l, 2p9n, 2p9p, 2p9s, 2p9u

Identifiers

Symbol(s)

ACTR3; ARP3

External IDs

OMIM: 604222 MGI: 1921367 HomoloGene: 68483

Gene ontology
Molecular Function:	• nucleotide binding • structural molecule activity • protein binding • ATP binding
Cellular Component:	• Arp2/3 protein complex • lamellipodium
Biological Process:	• cell motility

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_005721 (mRNA)
NP_005712 (protein)

NM_023735 (mRNA)
NP_076224 (protein)

Location

Chr 2: 114.36 - 114.43 Mb

Chr 1: 127.22 - 127.26 Mb

Pubmed search

[1]

[2]

ARP3 actin-related protein 3 homolog (yeast), also known as ACTR3, is a human gene.

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.^[1]

[edit] References

^ Entrez Gene: ACTR3 ARP3 actin-related protein 3 homolog (yeast).

[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. PMID 9210376.
Welch MD, DePace AH, Verma S, et al. (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. PMID 9230079.
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 ( Pt 1): 105–12. PMID 9359840.
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. PMID 9860974.
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. 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. 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. 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. 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. PMID 11018051.
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. 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. PMID 11741539.
Andersen JS, Lyon CE, Fox AH, et al. (2002). "Directed proteomic analysis of the human nucleolus.". Curr. Biol. 12 (1): 1–11. 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. PMID 11882288.