ACTR2

Available structures

Ortholog search: PDBe RCSB

List of PDB id codes
2P9N, 1TYQ, 1U2V, 4JD2, 3DXK, 3UKU, 3UKR, 2P9P, 2P9U, 3ULE, 3RSE, 2P9S, 2P9I, 4XF2, 2P9L, 1K8K, 3DXM, 4XEI

Identifiers

Aliases

ACTR2, ARP2, ARP2 actin-related protein 2 homolog (yeast), ARP2 actin related protein 2 homolog

External IDs

MGI: 1913963 HomoloGene: 4181 GeneCards: ACTR2

Gene ontology
Molecular function	• nucleotide binding • actin filament binding • structural constituent of cytoskeleton • actin binding • ATP binding • cytoskeletal protein binding
Cellular component	• cytoplasm • cytosol • cell projection • membrane • focal adhesion • Arp2/3 protein complex • cell cortex • actin cytoskeleton • actin cap • extracellular exosome • cytoskeleton • extracellular region • postsynaptic density of dendrite • lamellipodium • azurophil granule lumen • invadopodium • ficolin-1-rich granule lumen • podosome core
Biological process	• movement of cell or subcellular component • cytosolic transport • Fc-gamma receptor signaling pathway involved in phagocytosis • actin filament organization • ephrin receptor signaling pathway • meiotic chromosome movement towards spindle pole • meiotic cytokinesis • establishment or maintenance of cell polarity • meiotic cell cycle • asymmetric cell division • Arp2/3 complex-mediated actin nucleation • spindle localization • actin cytoskeleton organization • associative learning • response to immobilization stress • cellular response to trichostatin A • neutrophil degranulation • response to ethanol • cilium morphogenesis • positive regulation of dendritic spine morphogenesis • membrane organization
Sources:Amigo / QuickGO

Orthologs

Species

Human

Mouse

Entrez


10097


66713

Ensembl


ENSG00000138071


ENSMUSG00000020152

UniProt


P61160


P61161

RefSeq (mRNA)


NM_005722 NM_001005386


NM_146243

RefSeq (protein)


NP_001005386 NP_005713


NP_666355

Location (UCSC)

Chr 2: 65.23 – 65.27 Mb

Chr 11: 20.06 – 20.11 Mb

PubMed search

^[1]

^[2]

Wikidata

View/Edit Human

View/Edit Mouse

Actin-related protein 2 is a protein that in humans is encoded by the ACTR2 gene.^[3]

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.^[4]

References

↑ "Human PubMed Reference:".
↑ "Mouse PubMed Reference:".
↑ 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. PMC 2138188 . PMID 9230079. doi:10.1083/jcb.138.2.375.
↑ "Entrez Gene: ACTR2 ARP2 actin-related protein 2 homolog (yeast)".

Bearer EL, Prakash JM, Li Z (2002). "Actin dynamics in platelets.". Int. Rev. Cytol. 217: 137–82. PMC 3376087 . PMID 12019562. doi:10.1016/S0074-7696(02)17014-8.
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. PMID 9000076. doi:10.1038/385265a0.
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. doi:10.1016/S0960-9822(06)00223-5.
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. PMC 1218893 . 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. doi:10.1016/S0960-9822(98)00015-3.
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. PMID 10381382. doi:10.1006/bbrc.1999.0894.
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. doi:10.1016/S0960-9822(99)80337-6.
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. PMID 10524632. doi:10.1038/44183.
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. doi:10.1021/bi991843.
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. PMID 10781580. doi:10.1074/jbc.M000687200.
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. PMC 2189811 . PMID 11018051. doi:10.1083/jcb.151.1.29.
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. doi:10.1126/science.290.5492.801.
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. PMID 11146629. doi:10.1038/35050590.
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. PMID 11162547. doi:10.1006/bbrc.2000.4151.
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. PMC 2198874 . PMID 11706047. doi:10.1083/jcb.200105148.
Robinson RC, Turbedsky K, Kaiser DA, et al. (2001). "Crystal structure of Arp2/3 complex.". Science. 294 (5547): 1679–84. PMID 11721045. doi:10.1126/science.1066333.
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. doi:10.1016/S1097-2765(01)00393-8.
Li Z, Kim ES, Bearer EL (2002). "Arp2/3 complex is required for actin polymerization during platelet shape change.". Blood. 99 (12): 4466–74. PMC 3376088 . PMID 12036877. doi:10.1182/blood.V99.12.4466.

External links

ACTR2 human gene location in the UCSC Genome Browser.
ACTR2 human gene details in the UCSC Genome Browser.

PDB gallery

1k8k: Crystal Structure of Arp2/3 Complex
1tyq: Crystal structure of Arp2/3 complex with bound ATP and calcium
1u2v: Crystal structure of Arp2/3 complex with bound ADP and calcium
2p9i: Crystal Structure of bovine Arp2/3 Complex co-crystallized with ADP and crosslinked with gluteraldehyde
2p9k: Crystal structure of bovine Arp2/3 complex co-crystallized with ATP and crosslinked with glutaraldehyde
2p9l: Crystal Structure of bovine Arp2/3 complex
2p9n: Crystal Structure of bovine Arp2/3 complex co-crystallized with ADP
2p9p: Crystal Structure of bovine Arp2/3 complex co-crystallized with ADP
2p9s: Structure of bovine Arp2/3 complex co-crystallized with ATP/Mg2+
2p9u: Crystal structure of bovine Arp2/3 complex co-crystallized with AMP-PNP and calcium

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ACTR2

References

Further reading

External links