ACTR2

ACTR2
Available structures
PDB	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 location (Human)
Chr.	Chromosome 2 (human)[1]
End	65,271,253 bp[1]
Gene location (Mouse)
Chr.	Chromosome 11 (mouse)[2]
End	20,112,913 bp[2]
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; • 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
	10097
	66713
	ENSG00000138071
	ENSMUSG00000020152
	P61160
	P61161
	NM_005722; NM_001005386
	NM_146243; NM_001362899
	NP_001005386; NP_005713
	NP_666355; NP_001349828
	Wikidata
View/Edit Human	View/Edit Mouse

Actin-related protein 2 is a protein that in humans is encoded by the ACTR2 gene.^[5]

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.^[6]

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000138071 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000020152 - Ensembl, May 2017
↑ "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. doi:10.1083/jcb.138.2.375. PMC 2138188. PMID 9230079.
↑ "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. doi:10.1016/S0074-7696(02)17014-8. PMC 3376087. 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. 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. ( 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. 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.
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.
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.
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. PMC 2198874. 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. doi:10.1016/S1097-2765(01)00393-8. 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. doi:10.1182/blood.V99.12.4466. PMC 3376088. PMID 12036877.

External links

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

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000138071 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000020152 - Ensembl, May 2017

[3] "Human PubMed Reference:".

[4] "Mouse PubMed Reference:".

[pmid9230079-5] 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.

[entrez-6] "Entrez Gene: ACTR2 ARP2 actin-related protein 2 homolog (yeast)".

ACTR2

References

Further reading

External links