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Activation by Cdc42 and Pip2 of Wiskott-Aldrich Syndrome Protein (Wasp) Stimulates Actin Nucleation by Arp2/3 Complex

Higgs, Henry N., Pollard, Thomas D.·2000·The Journal of Cell Biology
DOI 10.1083/jcb.150.6.1311PMC PMC2150692
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Abstract

We purified native WASp (Wiskott-Aldrich Syndrome protein) from bovine thymus and studied its ability to stimulate actin nucleation by Arp2/3 complex. WASp alone is inactive in the presence or absence of 0.5 μM GTP-Cdc42. Phosphatidylinositol 4,5 bisphosphate (PIP2) micelles allowed WASp to activate actin nucleation by Arp2/3 complex, and this was further enhanced twofold by GTP-Cdc42. Filaments nucleated by Arp2/3 complex and WASp in the presence of PIP2 and Cdc42 concentrated around lipid micelles and vesicles, providing that Cdc42 was GTP-bound and prenylated. Thus, the high concentration of WASp in neutrophils (9 μM) is dependent on interactions with both acidic lipids and GTP-Cdc42 to activate actin nucleation by Arp2/3 complex. The results also suggest that membrane binding increases the local concentrations of Cdc42 and WASp, favoring their interaction.

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  • Several WASP family members contain PIP-interacting motifs that impact their localization and activation state.

    “several WASP family members including WASP/N-WASP, WAVE proteins, and WHAMM, all contain PIP-interacting motifs that impact their localization and activation state62–66.”

    From Endosomal PI(3)P regulation by the COMMD/CCDC22/CCDC93 (CCC) complex controls membrane protein recycling (2019) · cites this paper as [63]

    The Introduction reports that PIP2 stimulates WASp activation, and the Discussion proposes a role for PIP2-dependent membrane binding. But the Discussion explicitly says the PIP2-binding site on WASp is unknown, so this paper does not establish a PIP-interacting motif that controls localization. It also does not establish the claim for WAVE proteins or WHAMM. (LLM, conf=0.86)

    Experimental — accuracy not yet measured

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Research works printed but not linked: 52

  1. Abdul-Manan, 1999, Structure of Cdc42 in complex with the GTPase-binding domain of the ‘Wiskott-Aldrich Syndrome’ protein, Nature, 399, 379, 10.1038/20726 · DOI
  2. Bailly, 1999, Relationship between Arp2/3 complex and the barbed ends of actin filaments at the leading edge of carcinoma cells after epidermal growth factor stimulation, J. Cell Biol., 145, 331, 10.1083/jcb.145.2.331 · DOI
  3. Balasubramanian, 1996, Fission yeast Sop2pa novel and evolutionarily conserved protein that interacts with Arp3p and modulates profilin function, EMBO (Eur. Mol. Biol. Organ.) J., 15, 6426, 10.1002/j.1460-2075.1996.tb01034.x · DOI
  4. Blanchoin, 1998, Interaction of actin monomers with Acanthamoeba actophorin (ADF/cofilin) and profilin, J. Biol. Chem., 273, 25106, 10.1074/jbc.273.39.25106 · DOI
  5. Blanchoin, 2000, Direct observation of dendritic actin filament networks nucleated by Arp2/3 complex and WASp/Scar proteins, Nature, 404, 1007, 10.1038/35010008 · DOI · Paper page
  6. Cameron, 1999, Motility of ActA protein-coated microspheres driven by actin polymerization, Proc. Natl. Acad. Sci. USA, 96, 4908, 10.1073/pnas.96.9.4908 · DOI
  7. Carlier, 2000, Grb2 links signalling 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, 21946, 10.1074/jbc.M000687200 · DOI
  8. Egile, 1999, 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, 1319, 10.1083/jcb.146.6.1319 · DOI
  9. Fedorov, 1999, Structure of EVH1, a novel proline-rich ligand-binding module involved in cytoskeletal dynamics and neural function, Nat. Struct. Biol., 6, 661, 10.1038/10717 · DOI
  10. Frischknecht, 1999, Actin-based motility of vaccinia virus mimics receptor tyrosine kinase signalling, Nature, 401, 926, 10.1038/44860 · DOI
  11. Heyworth, 1993, Requirement for posttranslational processing of Rac GTP-binding proteins for activation of human neutrophil NADPH oxidase, Mol. Biol. Cell, 4, 261, 10.1091/mbc.4.3.261 · DOI
  12. Higgs, 1999, Regulation of actin polymerization by Arp2/3 complex and WASp/Scar proteins, J. Biol. Chem., 274, 32531, 10.1074/jbc.274.46.32531 · DOI
  13. Higgs, 1999, Influence of the Wiskott-Aldrich syndrome protein (WASp) C terminus and Arp2/3 complex on actin polymerization, Biochemistry, 38, 15212, 10.1021/bi991843+ · DOI
  14. Johnson, 1981, Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques, Biophys. J., 36, 575, 10.1016/S0006-3495(81)84753-4 · DOI
  15. Kim, 2000, Autoinhibition and activation mechanisms of the Wiskott-Aldrich Syndrome protein, Nature, 404, 151, 10.1038/35004513 · DOI
  16. Ma, 1998, Corequirement of specific phosphoinositides and small GTP-binding protein Cdc42 in inducing actin assembly in Xenopus egg extracts, J. Cell Biol., 140, 1125, 10.1083/jcb.140.5.1125 · DOI
  17. Ma, 1998, The Arp2/3 complex mediates actin polymerization induced by the small GTP-binding protein Cdc42, Proc. Natl. Acad. Sci. USA., 95, 15362, 10.1073/pnas.95.26.15362 · DOI
  18. Machesky, 1998, Scar1 and the related Wiskott-Aldrich syndrome protein WASP regulate the actin cytoskeleton through the Arp2/3 complex, Curr. Biol., 8, 1347, 10.1016/S0960-9822(98)00015-3 · DOI
  19. Machesky, 1994, Purification of a cortical complex containing two unconventional actins from Acanthamoeba by affinity chromatography on profilin agarose, J. Cell Biol., 127, 107, 10.1083/jcb.127.1.107 · DOI
  20. Machesky, 1997, Mammalian actin-related protein 2/3 complex localizes to regions of lamellipodial protrusion and is composed of evolutionarily conserved proteins, Biochem J., 328, 105, 10.1042/bj3280105 · DOI
  21. Machesky, 1999, Scar, a WASp-related protein, activates nucleation of actin filaments by the Arp2/3 complex, Proc. Natl. Acad. Sci. USA, 96, 3739, 10.1073/pnas.96.7.3739 · DOI · Paper page
  22. MacLean-Fletcher, 1980, Identification of a factor in conventional muscle actin preparation which inhibits actin filament self-association, Biochem. Biophys. Res. Commun., 96, 18, 10.1016/0006-291X(80)91175-4 · DOI
  23. McCollum, 1996, The Schizosaccharomyces pombe actin-related protein, Arp3, is a component of the cortical actin cytoskeleton and interacts with profilin, EMBO (Eur. Mol. Biol. Organ.) J., 15, 6438, 10.1002/j.1460-2075.1996.tb01035.x · DOI
  24. Merrifield, 1999, Endocytic vesicles move at the tips of actin tails in cultured mast cells, Nat. Cell Biol., 1, 72, 10.1038/9048 · DOI
  25. Miki, 1996, N-WASP, a novel actin-depolymerizing protein, regulates the cortical cytoskeletal rearrangement in a PIP2-dependent manner downstream of tyrosine kinases, EMBO (Eur. Mol. Biol. Organ.) J., 15, 5326, 10.1002/j.1460-2075.1996.tb00917.x · DOI
  26. Miki, 1998, Induction of filopodium formation by a WASP-related actin-depolymerizing protein N-WASP, Nature, 391, 93, 10.1038/34208 · DOI
  27. Moreau, 1998, Cdc42 is required for membrane dependent actin polymerization in vitro, FEBS (Fed. Eur. Biochem. Soc.) Lett., 427, 353, 10.1016/S0014-5793(98)00443-8 · DOI
  28. Morrell, 1999, A mutant of Arp2p causes partial disassembly of the Arp2/3 complex and loss of cortical actin function in fission yeast, Mol. Biol. Cell, 10, 4201, 10.1091/mbc.10.12.4201 · DOI
  29. Mullins, 1999, Rho-family GTPases require the Arp2/3 complex to stimulate actin polymerization in Acanthamoeba extracts, Curr. Biol., 9, 405, 10.1016/S0960-9822(99)80187-0 · DOI
  30. Mullins, 1998, The interaction of Arp2/3 complex with actinnucleation, high-affinity pointed end capping, and formation of branching networks of filaments, Proc. Natl. Acad. Sci. USA, 95, 6181, 10.1073/pnas.95.11.6181 · DOI
  31. Nobes, 1995, Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia, Cell, 81, 53, 10.1016/0092-8674(95)90370-4 · DOI
  32. Nomanbhoy, 1999, Kinetics of Cdc42 membrane extraction by Rho-GDI monitored by real-time fluorescence resonance energy transfer, Biochemistry, 38, 1744, 10.1021/bi982198u · DOI
  33. Ochs, 1998, The Wiskott-Aldrich Syndrome, Semin. Hematol., 35, 332
  34. Pollard, 1984, Quantitative analysis of the effect of Acanthamoeba profilin on actin filament nucleation and elongation, Biochemistry, 23, 6631, 10.1021/bi00321a054 · DOI
  35. Prehoda, 1999, Structure of the Enabled/VASP Homology 1 domain-peptide complexa key component in the spatial control of actin assembly, Cell, 97, 471, 10.1016/S0092-8674(00)80757-6 · DOI
  36. Regazzi, 1992, The small GTP-binding proteins in the cytosol of insulin-secreting cells are complexed to GDP dissociation inhibitor proteins, J. Biol. Chem., 267, 17512, 10.1016/S0021-9258(19)37072-3 · DOI
  37. Rohatgi, 1999, The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly, Cell, 97, 221, 10.1016/S0092-8674(00)80732-1 · DOI
  38. Spudich, 1971, The regulation of rabbit skeletal muscle contraction. I. Biochemical studies of the interaction of the tropomyosin-troponin complex with actin and the proteolytic fragments of myosin, J. Biol. Chem., 246, 4866, 10.1016/S0021-9258(18)62016-2 · DOI
  39. Suetsugu, 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, 296, 10.1006/bbrc.1999.0894 · DOI · Paper page
  40. Svitkina, 1999, Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia, J. Cell Biol., 145, 1009, 10.1083/jcb.145.5.1009 · DOI
  41. Taunton, 2000, Actin-dependent propulsion of endosomes and lysosomes by recruitment of N-WASP, J. Cell Biol., 148, 519, 10.1083/jcb.148.3.519 · DOI
  42. Ting-Beall, 1993, Volume and osmotic properties of human neutrophils, Blood, 81, 2774, 10.1182/blood.V81.10.2774.2774 · DOI
  43. Vinson, 1998, Interactions of Acanthamoeba profilin with actin and nucleotides bound to actin, Biochemistry, 37, 10871, 10.1021/bi980093l · DOI
  44. Weiner, 1999, Spatial control of actin polymerization during neutrophil chemotaxis, Nat. Cell Biol., 1, 75, 10.1038/10042 · DOI
  45. Welch, 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, 375, 10.1083/jcb.138.2.375 · DOI
  46. Welch, 1997, Actin polymerization is induced by Arp2/3 protein complex at the surface of Listeria monocytogenes, Nature, 385, 265, 10.1038/385265a0 · DOI
  47. Welch, 1998, Interaction of human Arp2/3 complex and the Listeria monocytogenes ActA protein in actin filament nucleation, Science, 281, 105, 10.1126/science.281.5373.105 · DOI
  48. Winter, 1999, Activation of the yeast Arp2/3 complex by Bee1p, a WASP-family protein, Curr. Biol., 9, 501, 10.1016/S0960-9822(99)80218-8 · DOI
  49. Winter, 1999, Genetic dissection of the budding yeast Arp2/3 complexa comparison of the in vivo and structural roles of individual subunits, Proc. Natl. Acad. Sci. USA, 96, 7288, 10.1073/pnas.96.13.7288 · DOI
  50. Yarar, 1999, The Wiskott-Aldrich syndrome protein directs actin-based motility by stimulating actin nucleation with the Arp2/3 complex, Curr. Biol., 9, 555, 10.1016/S0960-9822(99)80243-7 · DOI
  51. Zhu, 1996, Wiskott-Aldrich syndrome/X-linked thrombocytopeniaWASp gene mutations, protein expression, and phenotype, Blood, 90, 2680, 10.1182/blood.V90.7.2680 · DOI
  52. Zigmond, 1997, Regulation of actin polymerization in cell-free systems by GTPγS and Cdc42, J. Cell Biol., 138, 363, 10.1083/jcb.138.2.363 · DOI

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Metadata

Authors
Higgs, H. N., & Pollard, T. D.
Venue
The Journal of Cell Biology
Publisher
Rockefeller University Press
Published
2000-09-18
Volume
150
Issue
6
Pages
1311-1320
ISSN
  • 0021-9525
  • 1540-8140
DOI
10.1083/jcb.150.6.1311
PMC
PMC2150692
Cited by
446
References
1
Language
en

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