ACTR2

Nowadays, ACTR2 is a topic on everyone's lips. From its impact on society to its implications on the global economy, ACTR2 has captured the attention of experts and citizens alike. With endless opinions and analyzes ranging from the most technical to the most emotional, there is no doubt that ACTR2 has become a point of debate and reflection for today's society. In this article, we will explore the different facets of ACTR2, examining both its positive and negative aspects, with the aim of providing a complete and enriching overview of this topic.

Mammalian protein found in Homo sapiens

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, actin related protein 2, Actin related protein 2/3 complex subunit 2, p34-ARC, ARPC2, arp2/3 complex 34 kDa subunit, testis tissue sperm-binding protein Li 53e, actin related protein 2/3 complex, subunit 2, 34kDa, ARP2/3 protein complex subunit 34, actin-related protein 2/3 complex subunit 2
External IDs	OMIM: 604221; MGI: 1913963; HomoloGene: 4181; GeneCards: ACTR2; OMA:ACTR2 - orthologs
Gene location (Human) Chr. Chromosome 2 (human)[1] Band 2p14 Start 65,227,788 bp[1] End 65,271,253 bp[1]
Gene location (Mouse) Chr. Chromosome 11 (mouse)[2] Band 11 A3.1|11 12.88 cM Start 20,012,304 bp[2] End 20,062,913 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in monocyte trabecular bone epithelium of nasopharynx appendix palpebral conjunctiva lymph node mucosa of sigmoid colon bone marrow visceral pleura bone marrow cell Top expressed in stroma of bone marrow granulocyte tibiofemoral joint medial dorsal nucleus dorsal striatum trigeminal ganglion globus pallidus blood nucleus of stria terminalis amygdala More reference expression data BioGPS n/a
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 ficolin-1-rich granule lumen podosome core Biological process 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 meiosis 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 assembly 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 NM_001362899 RefSeq (protein) NP_001005386 NP_005713 NP_666355 NP_001349828 Location (UCSC) Chr 2: 65.23 – 65.27 Mb Chr 11: 20.01 – 20.06 Mb PubMed search [3] [4]
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 ACTR2 has not yet been determined. However, it 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. ^ ^{a b c} GRCh38: Ensembl release 89: ENSG00000138071 – Ensembl, May 2017
2. ^ ^{a b c} GRCm38: Ensembl release 89: ENSMUSG00000020152 – Ensembl, May 2017
3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
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.
6. ^ "Entrez Gene: ACTR2 ARP2 actin-related protein 2 homolog (yeast)".

Further reading

• Bearer EL, Prakash JM, Li Z (2002). "Actin dynamics in platelets". Int. Rev. Cytol. International Review of Cytology. 217: 137–82. doi:10.1016/S0074-7696(02)17014-8. ISBN 9780123646217. 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. Bibcode:1997Natur.385..265W. doi:10.1038/385265a0. PMID 9000076. S2CID 4358529.
• 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. Bibcode:1997CBio....7..519W. doi:10.1016/S0960-9822(06)00223-5. PMID 9210376. S2CID 52837402.
• 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) (Pt 1): 105–12. doi:10.1042/bj3280105. 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. S2CID 16661755.
• 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. Bibcode:1999CBio....9..759M. doi:10.1016/S0960-9822(99)80337-6. PMID 10421578. S2CID 17030983.
• 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. Bibcode:1999Natur.401..613L. doi:10.1038/44183. PMID 10524632. S2CID 4313372.
• 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. Bibcode:2000Sci...290..801P. 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. S2CID 30437883.
• 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. Bibcode:2001Sci...294.1679R. doi:10.1126/science.1066333. PMID 11721045. S2CID 18088124.
• 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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