Biology:ACTR3
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Short description: Mammalian protein found in Homo sapiens
![]() Generic protein structure example |
Actin-related protein 3 is a protein that in humans is encoded by the ACTR3 gene.[1]
Function
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.[2]
Interactions
ACTR3 has been shown to interact with Cortactin.[3][4]
References
- ↑ "The human Arp2/3 complex is composed of evolutionarily conserved subunits and is localized to cellular regions of dynamic actin filament assembly". The Journal of Cell Biology 138 (2): 375–84. Jul 1997. doi:10.1083/jcb.138.2.375. PMID 9230079.
- ↑ "Entrez Gene: ACTR3 ARP3 actin-related protein 3 homolog (yeast)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10096.
- ↑ "Cortactin localization to sites of actin assembly in lamellipodia requires interactions with F-actin and the Arp2/3 complex". The Journal of Cell Biology 151 (1): 29–40. Oct 2000. doi:10.1083/jcb.151.1.29. PMID 11018051.
- ↑ "Osmotic stress-induced remodeling of the cortical cytoskeleton". American Journal of Physiology. Cell Physiology 283 (3): C850–65. Sep 2002. doi:10.1152/ajpcell.00018.2002. PMID 12176742.
Further reading
- "Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes". Nature 385 (6613): 265–9. Jan 1997. doi:10.1038/385265a0. PMID 9000076. Bibcode: 1997Natur.385..265W.
- "The complex containing actin-related proteins Arp2 and Arp3 is required for the motility and integrity of yeast actin patches". Current Biology 7 (7): 519–29. Jul 1997. doi:10.1016/S0960-9822(06)00223-5. PMID 9210376.
- "Mammalian actin-related protein 2/3 complex localizes to regions of lamellipodial protrusion and is composed of evolutionarily conserved proteins". The Biochemical Journal 328 (1): 105–12. Nov 1997. doi:10.1042/bj3280105. PMID 9359840.
- "The Arp2/3 complex mediates actin polymerization induced by the small GTP-binding protein Cdc42". Proceedings of the National Academy of Sciences of the United States of America 95 (26): 15362–7. Dec 1998. doi:10.1073/pnas.95.26.15362. PMID 9860974. Bibcode: 1998PNAS...9515362M.
- "Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex". Current Biology 8 (25): 1347–56. 1999. doi:10.1016/S0960-9822(98)00015-3. PMID 9889097.
- "Identification of two human WAVE/SCAR homologues as general actin regulatory molecules which associate with the Arp2/3 complex". Biochemical and Biophysical Research Communications 260 (1): 296–302. Jun 1999. doi:10.1006/bbrc.1999.0894. PMID 10381382.
- "The Arp2/3 complex is essential for the actin-based motility of Listeria monocytogenes". Current Biology 9 (14): 759–62. Jul 1999. doi:10.1016/S0960-9822(99)80337-6. PMID 10421578.
- "Reconstitution of actin-based motility of Listeria and Shigella using pure proteins". Nature 401 (6753): 613–6. Oct 1999. doi:10.1038/44183. PMID 10524632. Bibcode: 1999Natur.401..613L.
- "Influence of the C terminus of Wiskott-Aldrich syndrome protein (WASp) and the Arp2/3 complex on actin polymerization". Biochemistry 38 (46): 15212–22. Nov 1999. doi:10.1021/bi991843. PMID 10563804.
- "GRB2 links signaling to actin assembly by enhancing interaction of neural Wiskott-Aldrich syndrome protein (N-WASp) with actin-related protein (ARP2/3) complex". The Journal of Biological Chemistry 275 (29): 21946–52. Jul 2000. doi:10.1074/jbc.M000687200. PMID 10781580.
- "ARP3beta, the gene encoding a new human actin-related protein, is alternatively spliced and predominantly expressed in brain neuronal cells". European Journal of Biochemistry 267 (10): 2921–8. May 2000. doi:10.1046/j.1432-1327.2000.01306.x. PMID 10806390.
- "Cortactin localization to sites of actin assembly in lamellipodia requires interactions with F-actin and the Arp2/3 complex". The Journal of Cell Biology 151 (1): 29–40. Oct 2000. doi:10.1083/jcb.151.1.29. PMID 11018051.
- "Integration of multiple signals through cooperative regulation of the N-WASP-Arp2/3 complex". Science 290 (5492): 801–6. Oct 2000. doi:10.1126/science.290.5492.801. PMID 11052943. Bibcode: 2000Sci...290..801P.
- "Interaction of WASP/Scar proteins with actin and vertebrate Arp2/3 complex". Nature Cell Biology 3 (1): 76–82. Jan 2001. doi:10.1038/35050590. PMID 11146629.
- "Interactions among subunits of human Arp2/3 complex: p20-Arc as the hub". Biochemical and Biophysical Research Communications 280 (2): 513–7. Jan 2001. doi:10.1006/bbrc.2000.4151. PMID 11162547.
- "Crystal structure of Arp2/3 complex". Science 294 (5547): 1679–84. Nov 2001. doi:10.1126/science.1066333. PMID 11721045. Bibcode: 2001Sci...294.1679R.
- "Reconstitution of human Arp2/3 complex reveals critical roles of individual subunits in complex structure and activity". Molecular Cell 8 (5): 1041–52. Nov 2001. doi:10.1016/S1097-2765(01)00393-8. PMID 11741539.
- "Directed proteomic analysis of the human nucleolus". Current Biology 12 (1): 1–11. Jan 2002. doi:10.1016/S0960-9822(01)00650-9. PMID 11790298.
- "Cadherin-directed actin assembly: E-cadherin physically associates with the Arp2/3 complex to direct actin assembly in nascent adhesive contacts". Current Biology 12 (5): 379–82. Mar 2002. doi:10.1016/S0960-9822(02)00661-9. PMID 11882288.
External links
- ACTR3 human gene location in the UCSC Genome Browser.
- ACTR3 human gene details in the UCSC Genome Browser.
![]() | Original source: https://en.wikipedia.org/wiki/ACTR3.
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