The Diverse Family of Arp2/3 Complexes

Trends in Cell Biology

Volumn 27, Issue 2, 2017, Pages 93-100

  Pizarro Cerdá, Javier ^a,b,c   Chorev, Dror Shlomo ^d,e   Geiger, Benjamin ^d   Cossart, Pascale ^a,b,c  

^a INSTITUT PASTEUR   (France)

^b INSERM   (France)

^c USC 2020   (France)

^d WEIZMANN INSTITUTE OF SCIENCE   (Israel)

^e UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

actin polymerization; Arp2 3; focal adhesions; Listeria monocytogenes; vaccinia virus

Indexed keywords

ACTIN RELATED PROTEIN 2-3 COMPLEX;

FOCAL ADHESION; HUMAN; LISTERIOSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN FUNCTION; REVIEW; VACCINIA VIRUS; ANIMAL; BIOLOGICAL MODEL; METABOLISM; MULTIGENE FAMILY;

ACTIN-RELATED PROTEIN 2-3 COMPLEX; ANIMALS; HUMANS; MODELS, BIOLOGICAL; MULTIGENE FAMILY;

EID: 84996931883     PISSN: 09628924     EISSN: 18793088     Source Type: Journal    
DOI: 10.1016/j.tcb.2016.08.001     Document Type: Review

References (70)

1. 1 Fletcher, D.A., Mullins, R.D., Cell mechanics and the cytoskeleton. Nature 463 (2010), 485–492.
2. 2 Pollard, T.D., Cooper, J.A., Actin, a central player in cell shape and movement. Science 326 (2009), 1208–1212.
3. 3 Berriman, M., et al. The genome of the African trypanosome Trypanosoma brucei. Science 309 (2005), 416–422.
4. 4 Goley, E.D., Welch, M.D., The ARP2/3 complex: an actin nucleator comes of age. Nat. Rev. Mol. Cell Biol. 7 (2006), 713–726.
5. 5 Krause, M., Gautreau, A., Steering cell migration: lamellipodium dynamics and the regulation of directional persistence. Nat. Rev. Mol. Cell Biol. 15 (2014), 577–590.
6. 6 Campellone, K.G., Welch, M.D., A nucleator arms race: cellular control of actin assembly. Nat. Rev. Mol. Cell Biol. 11 (2010), 237–251.
7. 7 Pollard, T.D., Beltzner, C.C., Structure and function of the Arp2/3 complex. Curr. Opin. Struct. Biol. 12 (2002), 768–774.
8. 8 Chorev, D.S., et al. Regulation of focal adhesion formation by a vinculin-Arp2/3 hybrid complex. Nat. Commun. 5 (2014), 1–11.
9. 9 Kühbacher, A., et al. Genome-wide siRNA screen identifies complementary signaling pathways involved in Listeria infection and reveals different actin nucleation mechanisms during Listeria cell invasion and actin comet tail formation. mBio 6 (2015), e00598–e615.
10. 10 Abella, J.V.G., et al. Isoform diversity in the Arp2/3 complex determines actin filament dynamics. Nat. Cell Biol. 18 (2015), 76–86.
11. 11 Machesky, L.M., et al. Purification of a cortical complex containing two unconventional actins from Acanthamoeba by affinity chromatography on profilin-agarose. J. Cell Biol. 127 (1994), 107–115.
12. 12 Balasubramanian, M.K., et al. Fission yeast Sop2p: a novel and evolutionarily conserved protein that interacts with Arp3p and modulates profilin function. EMBO J. 15 (1996), 6426–6437.
13. 13 Winter, D., et al. The complex containing actin-related proteins Arp2 and Arp3 is required for the motility and integrity of yeast actin patches. Curr. Biol. 7 (1997), 519–529.
14. 14 Welch, M.D., et al. 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 (1997), 375–384.
15. 15 Welch, M.D., et al. Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes. Nature 385 (1997), 265–269.
16. 16 Kocks, C., et al. L. monocytogenes-induced actin assembly requires the actA gene product, a surface protein. Cell 68 (1992), 521–531.
17. 17 Welch, M.D., et al. Interaction of human Arp2/3 complex and the Listeria monocytogenes ActA protein in actin filament nucleation. Science 281 (1998), 105–108.
18. 18 Yarar, D., et al. The Wiskott–Aldrich syndrome protein directs actin-based motility by stimulating actin nucleation with the Arp2/3 complex. Curr. Biol. 9 (1999), 555–558.
19. 19 Rohatgi, R., et al. The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly. Cell 97 (1999), 221–231.
20. 20 Machesky, L.M., et al. Scar, a WASp-related protein, activates nucleation of actin filaments by the Arp2/3 complex. Proc. Natl. Acad. Sci. U.S.A. 96 (1999), 3739–3744.
21. 21 Mullins, R.D., et al. The interaction of Arp2/3 complex with actin: nucleation, high affinity pointed end capping, and formation of branching networks of filaments. Proc. Natl. Acad. Sci. U.S.A. 95 (1998), 6181–6186.
22. 22 Svitkina, T.M., Borisy, G.G., Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia. J. Cell Biol. 145 (1999), 1009–1026.
23. 23 Blanchoin, L., et al. Direct observation of dendritic actin filament networks nucleated by Arp2/3 complex and WASP/Scar proteins. Nature 404 (2000), 1007–1011.
24. 24 Cossart, P., Actin-based motility of pathogens: the Arp2/3 complex is a central player. Cell Microbiol. 2 (2000), 195–205.
25. 25 Pizarro-Cerdá, J., et al. Entry of Listeria monocytogenes in mammalian epithelial cells: an updated view. Cold Spring Harb. Perspect. Med., 2, 2012, a010009.
26. 26 Bierne, H., et al. A role for cofilin and LIM kinase in Listeria-induced phagocytosis. J. Cell Biol. 155 (2001), 101–112.
27. 27 Sousa, S., et al. Src, cortactin and Arp2/3 complex are required for E-cadherin-mediated internalization of Listeria into cells. Cell Microbiol. 9 (2007), 2629–2643.
28. 28 Egile, C., et al. Activation of the CDC42 effector N-WASP by the Shigella flexneri IcsA protein promotes actin nucleation by Arp2/3 complex and bacterial actin-based motility. J. Cell. Biol. 146 (1999), 1319–1332.
29. 29 Bougnères, L., et al. Cortactin and Crk cooperate to trigger actin polymerization during Shigella invasion of epithelial cells. J. Cell. Biol. 166 (2004), 225–235.
30. 30 Suzuki, T., et al. Neural Wiskott–Aldrich syndrome protein is implicated in the actin-based motility of Shigella flexneri. EMBO J. 17 (1998), 2767–2776.
31. 31 Jeng, R.L., et al. A Rickettsia WASP-like protein activates the Arp2/3 complex and mediates actin-based motility. Cell Microbiol. 6 (2004), 761–769.
32. 32 Gouin, E., et al. The RickA protein of Rickettsia conorii activates the Arp2/3 complex. Nature 427 (2004), 457–461.
33. 33 Reed, S.C., et al. Rickettsia actin-based motility occurs in distinct phases mediated by different actin nucleators. Curr. Biol. 24 (2013), 98–103.
34. 34 Martinez, J.J., Early signaling events involved in the entry of Rickettsia conorii into mammalian cells. J. Cell Sci. 117 (2004), 5097–5106.
35. 35 Reed, S.C.O., et al. Rickettsia parkeri invasion of diverse host cells involves an Arp2/3 complex, WAVE complex and Rho-family GTPase-dependent pathway. Cell Microbiol. 14 (2012), 529–545.
36. 36 Cudmore, S., et al. Actin-based motility of vaccinia virus. Nature 378 (1995), 636–638.
37. 37 Frischknecht, F., et al. Actin-based motility of vaccinia virus mimics receptor tyrosine kinase signalling. Nature 401 (1999), 926–929.
38. 38 Stamm, L.M., et al. Mycobacterium marinum escapes from phagosomes and is propelled by actin-based motility. J. Exp. Med. 198 (2003), 1361–1368.
39. 39 Sitthidet, C., et al. Actin-based motility of Burkholderia thailandensis requires a central acidic domain of BimA that recruits and activates the cellular Arp2/3 complex. J. Bacteriol. 192 (2010), 5249–5252.
40. 40 Gouin, E., et al. Actin-based motility of intracellular pathogens. Curr. Opin. Microbiol. 8 (2005), 35–45.
41. 41 Benanti, E.L., et al. Virulent Burkholderia species mimic host actin polymerases to drive actin-based motility. Cell 161 (2015), 348–360.
42. 42 Gouin, E., et al. Intracellular bacteria find the right motion. Cell 161 (2015), 199–200.
43. 43 Lees-Miller, J.P., et al. Identification of act2, an essential gene in the fission yeast Schizosaccharomyces pombe that encodes a protein related to actin. Proc. Natl. Acad. Sci. U.S.A. 89 (1992), 80–83.
44. 44 Winter, D.C., et al. Genetic dissection of the budding yeast Arp2/3 complex: a comparison of the in vivo and structural roles of individual subunits. Proc. Natl. Acad. Sci. U.S.A. 96 (1999), 7288–7293.
45. 45 Machesky, L.M., et al. Mammalian actin-related protein 2/3 complex localizes to regions of lamellipodial protrusion and is composed of evolutionarily conserved proteins. Biochem. J. 328 (1997), 105–112.
46. 46 May, R.C., et al. Involvement of the Arp2/3 complex in phagocytosis mediated by FcγR or CR3. Nat. Cell Biol. 2 (2000), 246–248.
47. 47 Luna, A., et al. Regulation of protein transport from the Golgi complex to the endoplasmic reticulum by CDC42 and N-WASP. Mol. Biol. Cell. 13 (2002), 866–879.
48. 48 Demali, K.A., et al. Recruitment of the Arp2/3 complex to vinculin: coupling membrane protrusion to matrix adhesion. J. Cell. Biol. 159 (2002), 881–891.
49. 49 Kolluri, R., et al. Direct interaction of the Wiskott–Aldrich syndrome protein with the GTPase Cdc42. Proc. Natl. Acad. Sci. U.S.A. 93 (1996), 5615–5618.
50. 50 Kirchhausen, T., Rosen, F.S., Disease mechanism: unravelling Wiskott–Aldrich syndrome. Curr. Biol. 6 (1996), 676–678.
51. 51 Volkmann, N., et al. Structure of Arp2/3 complex in its activated state and in actin filament branch junctions. Science 293 (2001), 2456–2459.
52. 52 Robinson, R.C., et al. Crystal structure of Arp2/3 complex. Science 294 (2001), 1679–1684.
53. 53 Gournier, H., et al. Reconstitution of human Arp2/3 complex reveals critical roles of individual subunits in complex structure and activity. Mol. Cell. 8 (2001), 1041–1052.
54. 54 Rouiller, I., et al. The structural basis of actin filament branching by the Arp2/3 complex. J. Cell Biol. 180 (2008), 887–895.
55. 55 Kelly, A.E., et al. Actin binding to the central domain of WASP/Scar proteins plays a critical role in the activation of the Arp2/3 complex. J. Biol. Chem. 281 (2006), 10589–10597.
56. 56 Vadlamudi, R.K., et al. p41-Arc subunit of human Arp2/3 complex is a p21-activated kinase-1-interacting substrate. EMBO Rep. 5 (2004), 154–160.
57. 57 LeClaire, L.L., et al. Phosphorylation of the Arp2/3 complex is necessary to nucleate actin filaments. J. Cell. Biol. 182 (2008), 647–654.
58. 58 Choi, C.H., et al. Phosphorylation of actin-related protein 2 (Arp2) is required for normal development and cAMP chemotaxis in Dictyostelium. J. Biol. Chem. 288 (2013), 2464–2474.
59. 59 Michard, C., et al. The Legionella kinase LegK2 targets the ARP2/3 complex to inhibit actin nucleation on phagosomes and allow bacterial evasion of the late endocytic pathway. mBio 6 (2015), e00354–e415.
60. 60 Jay, P., et al. ARP3β, the gene encoding a new human actin-related protein, is alternatively spliced and predominantly expressed in brain neuronal cells. Eur. J. Biochem. 267 (2000), 2921–2928.
61. 61 Laurila, E., et al. Characterization of the 7q21-q22 amplicon identifies ARPC1A, a subunit of the Arp2/3 complex, as a regulator of cell migration and invasion in pancreatic cancer. Genes Chromosom. Cancer 48 (2009), 330–339.
62. 62 Millard, T.H., et al. Identification and characterisation of a novel human isoform of Arp2/3 complex subunit p16-ARC/ARPC5. Cell Motil. Cytoskeleton 54 (2003), 81–90.
63. 63 Nolen, B.J., et al. Crystal structures of actin-related protein 2/3 complex with bound ATP or ADP. Proc. Natl. Acad. Sci. U.S.A. 101 (2004), 15627–15632.
64. 64 Campellone, K.G., et al. WHAMM is an Arp2/3 complex activator that binds microtubules and functions in ER to Golgi transport. Cell 134 (2008), 148–161.
65. 65 Zuchero, J.B., et al. p53-cofactor JMY is a multifunctional actin nucleation factor. Nat. Cell Biol. 11 (2009), 451–459.
66. 66 Rotty, J.D., et al. New insights into the regulation and cellular functions of the ARP2/3 complex. Nat. Rev. Mol. Cell Biol. 14 (2012), 7–12.
67. 67 Padrick, S.B., et al. Arp2/3 complex is bound and activated by two WASP proteins. Proc. Natl. Acad. Sci. U.S.A. 108 (2011), E472–E479.
68. 68 Egile, C., et al. Mechanism of filament nucleation and branch stability revealed by the structure of the Arp2/3 complex at actin branch junctions. PLoS Biol., 3, 2005, e383.
69. 69 Goley, E.D., et al. An actin-filament-binding interface on the Arp2/3 complex is critical for nucleation and branch stability. Proc. Natl. Acad. Sci. U.S.A. 107 (2010), 8159–8164.
70. 70 Balcer, H.I., et al. The p40/ARPC1 subunit of Arp2/3 complex performs multiple essential roles in WASp-regulated actin nucleation. J. Biol. Chem. 285 (2010), 8481–8491.