Structures of actin-bound Wiskott-Aldrich syndrome protein homology 2 (WH2) domains of Spire and the implication for filament nucleation

TD Pollard, JA Cooper, Actin, a central player in cell shape and movement. Science 27, 1208–1212 (2009).

D Sept, JA McCammon, Thermodynamics and kinetics of actin filament nucleation. Biophys J 81, 667–674 (2001).

MA Chesarone, BL Goode, Actin nucleation and elongation factors: Mechanisms and interplay. Curr Opin Cell Biol 21, 28–37 (2009).

RD Mullins, TD Pollard, Rho-family GTPases require the Arp2/3 complex to stimulate actin polymerization in Acanthamoeba extracts. Curr Biol 9, 405–415 (1999).

KG Campellone, NJ Webb, EA Znameroski, MD Welch, WHAMM is an Arp2/3 complex activator that binds microtubules and functions in ER to Golgi transport. Cell 134, 148–161 (2008).

R Liu, et al., Wash functions downstream of Rho and links linear and branched actin nucleation factors. Development 136, 2849–2860 (2009).

JB Zuchero, AS Coutts, ME Quinlan, NB Thangue, RD Mullins, p53-cofactor JMY is a multifunctional actin nucleation factor. Nat Cell Biol 11, 451–459 (2009).

KG Campellone, MD Welch, A nucleator arms race: Cellular control of actin assembly. Nat Rev Mol Cell Biol 11, 237–251 (2010).

M Evangelista, D Pruyne, DC Amberg, C Boone, A Bretscher, Formins direct Arp2/3-independent actin filament assembly to polarize cell growth in yeast. Nat Cell Biol 4, 32–41 (2002).

M Evangelista, S Zigmond, C Boone, Formins: signaling effectors for assembly and polarization of actin filaments. J Cell Sci 116, 2603–2611 (2003).

I Sagot, AA Rodal, J Moseley, BL Goode, D Pellman, An actin nucleation mechanism mediated by Bni1 and profilin. Nat Cell Biol 4, 626–631 (2002).

JB Xu, et al., Crystal structures of a formin homology-2 domain reveal a tethered dimer architecture. Cell 116, 711–723 (2004).

M Symons, et al., Wiskott-Aldrich syndrome protein, a novel effector for the GTPase CDC42Hs, is implicated in actin polymerization. Cell 84, 723–734 (1996).

B Qualmann, MM Kessels, New players in actin polymerization-WH2-domain-containing actin nucleators. Trends Cell Biol 19, 276–285 (2009).

M Pechlivanis, A Samol, E Kerkhoff, Identification of a short Spir interaction sequence at the C-terminal end of formin subgroup proteins. J Biol Chem 284, 25324–25333 (2009).

ME Quinlan, JE Heuser, E Kerkhoff, RD Mullins, Drosophila Spire is an actin nucleation factor. Nature 433, 382–388 (2005).

R Ahuja, et al., Cordon-Bleu is an actin nucleation factor and controls neuronal morphology. Cell 131, 337–350 (2007).

D Chereau, et al., Leiomodin is an actin filament nucleator in muscle cells. Science 320, 239–243 (2008).

TD Pollard, GG Borisy, Cellular motility driven by assembly and disassembly of actin filaments. Cell 112, 453–465 (2003).

RC Robinson, et al., Crystal structure of Arp2/3 complex. Science 294, 1679–1684 (2001).

T Otomo, et al., Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain. Nature 433, 488–494 (2005).

LJ Manseau, T Schupbach, Cappuccino and spire: two unique maternal-effect loci required for both the anteroposterior and dorsoventral patterns of the Drosophila embryo. Genes Dev 3, 1437–1452 (1989).

E Kerkhoff, et al., The Spir actin organizers are involved in vesicle transport processes. Curr Biol 11, 1963–1968 (2001).

AE Rosales-Nieves, et al., Coordination of microtubule and microfilament dynamics by Drosophila Rho1, Spire and Cappuccino. Nat Cell Biol 8, 367–376 (2006).

ME Quinlan, S Hilgert, A Bedrossian, RD Mullins, E Kerkhoff, Regulatory interactions between two actin nucleators, Spire and Cappuccino. J Cell Biol 179, 117–128 (2007).

M Bosch, et al., Analysis of the function of spire in actin assembly and its synergy with formin and profilin. Mol Cell 28, 555–568 (2007).

M Czisch, M Schleicher, S Horger, W Voelter, TA Holak, Conformation of thymosin beta 4 in water determined by NMR spectroscopy. Eur J Biochem 218, 335–344 (1993).

M Hertzog, et al., The β-thymosin/WH2 domain; structural basis for the switch from inhibition to promotion of actin assembly. Cell 117, 611–623 (2004).

E Irobi, et al., Structural basis of actin sequestration by thymosin β4: Implications for WH2 proteins. EMBO J 23, 3599–3608 (2004).

D Chereau, et al., Actin-bound structures of Wiskott-Aldrich syndrome protein (WASP) homology domain 2 and the implications for filament assembly. Proc Natl Acad Sci USA 102, 16644–16649 (2005).

AH Aguda, B Xue, E Irobi, T Preat, RC Robinson, The structural basis of actin interaction with multiple WH2/betathymosin motif-containing proteins. Structure 14, 469–476 (2006).

SH Lee, et al., Structural basis for the actin-binding function of missing-in-metastasis. Structure 15, 145–155 (2007).

MA Rould, Q Wan, PB Joel, S Lowey, KM Trybus, Crystal structures of expressed non-polymerizable monomeric actin in the ADP and ATP states. J Biol Chem 281, 31909–31919 (2006).

G Rebowski, et al., X-ray scattering study of actin polymerization nuclei assembled by tandem W domains. Proc Natl Acad Sci USA 105, 10785–10790 (2008).

P Graceffa, R Dominguez, Crystal structure of monomeric actin in the ATP state. Structural basis of nucleotide-dependent actin dynamics. J Biol Chem 278, 34172–34180 (2003).

KC Holmes, D Popp, W Gebhard, W Kabsch, Atomic model of the actin filament. Nature 347, 44–49 (1990).

T Oda, M Iwasa, T Aihara, Y Maeda, A Narita, The nature of the globular- to fibrous-actin transition. Nature 457, 441–445 (2009).

W Kabsch, Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J Appl Crystallogr 26, 795–800 (1993).