ACTR2

From Wikipedia, the free encyclopedia

ARP2 actin-related protein 2 homolog (yeast)

PDB rendering based on 1k8k.

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

Identifiers

Symbol(s)

ACTR2; ARP2

External IDs

OMIM: 604221 MGI: 1913963 HomoloGene: 4181

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

Orthologs

Human

Mouse

n/a

n/a

Refseq

NM_001005386 (mRNA)
NP_001005386 (protein)

NM_146243 (mRNA)
NP_666355 (protein)

Location

n/a

Chr 11: 19.96 - 20.01 Mb

Pubmed search

[1]

[2]

ARP2 actin-related protein 2 homolog (yeast), also known as ACTR2, 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. Two transcript variants encoding different isoforms have been found for this gene.^[1]

[edit] References

^ Entrez Gene: ACTR2 ARP2 actin-related protein 2 homolog (yeast).

[edit] Further reading

Bearer EL, Prakash JM, Li Z (2002). "Actin dynamics in platelets.". Int. Rev. Cytol. 217: 137–82. PMID 12019562.
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.
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.
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.
Flanagan LA, Chou J, Falet H, et al. (2001). "Filamin A, the Arp2/3 complex, and the morphology and function of cortical actin filaments in human melanoma cells.". J. Cell Biol. 155 (4): 511–7. doi:10.1083/jcb.200105148. PMID 11706047.
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.
Li Z, Kim ES, Bearer EL (2002). "Arp2/3 complex is required for actin polymerization during platelet shape change.". Blood 99 (12): 4466–74. PMID 12036877.