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Reliable, easy-to-read patient information on common medical conditions — written in plain language, free of jargon, and grounded in current evidence. Browse the most frequent diagnoses, understand what they mean for everyday life, and learn which steps and questions help you have a focused conversation with your doctor.

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ARPC5

Introduction

Actin-related protein 2/3 complex subunit 5 is a protein that in humans is encoded by the ARPC5 gene.[1][2][3]

Function

Function

This gene encodes one of seven subunits of the human Arp2/3 protein complex. The Arp2/3 protein complex has been implicated in the control of actin polymerization in cells and has been conserved through evolution. The exact role of the protein encoded by this gene, the p16 subunit, has yet to be determined.[3]

Interactions

Interactions

ARPC5 has been shown to interact with ARPC4.[4][5]

References

References

  1. ↑ Machesky LM, Reeves E, Wientjes F, Mattheyse FJ, Grogan A, Totty NF, Burlingame AL, Hsuan JJ, Segal AW (1997). “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) (1): 105–12. PMC 1218893. PMID 9359840.
  2. ↑ Welch MD, DePace AH, Verma S, Iwamatsu A, Mitchison TJ (August 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.
  3. ↑ 3.0 3.1 “Entrez Gene: ARPC5 actin related protein 2/3 complex, subunit 5, 16kDa”.
  4. ↑ Millard TH, Behrendt B, Launay S, Fütterer K, Machesky LM (2003). “Identification and characterisation of a novel human isoform of Arp2/3 complex subunit p16-ARC/ARPC5”. Cell Motil. Cytoskeleton. 54 (1): 81–90. doi:10.1002/cm.10087. PMID 12451597.
  5. ↑ 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.
Further reading

Further reading

  • 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.
  • Robinson RC, Turbedsky K, Kaiser DA, Marchand JB, Higgs HN, Choe S, Pollard TD (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, Trinh T, Welch MD (2001). “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.
  • Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J (2003). “Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides”. Nat. Biotechnol. 21 (5): 566–9. doi:10.1038/nbt810. PMID 12665801.
  • Singh S, Powell DW, Rane MJ, Millard TH, Trent JO, Pierce WM, Klein JB, Machesky LM, McLeish KR (2003). “Identification of the p16-Arc subunit of the Arp 2/3 complex as a substrate of MAPK-activated protein kinase 2 by proteomic analysis”. J. Biol. Chem. 278 (38): 36410–7. doi:10.1074/jbc.M306428200. PMID 12829704.
  • Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O’Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). “Large-scale mapping of human protein-protein interactions by mass spectrometry”. Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
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