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Skillman, K. M., Ma, C. I., Fremont, D. H., Diraviyam, K., Cooper, J. A., Sept, D., & Sibley, L. D. (2013). The unusual dynamics of parasite actin result from isodesmic polymerization. Nature Communications, 4(1).

Authors 7
  1. Kristen M. Skillman (first)
  2. Christopher I. Ma (additional)
  3. Daved H. Fremont (additional)
  4. Karthikeyan Diraviyam (additional)
  5. John A. Cooper (additional)
  6. David Sept (additional)
  7. L. David Sibley (additional)
References 41 Referenced 63
  1. Kabsch, W. & Holmes, K. C. The actin fold. FASEB J. 9, 167–174 (1995). (10.1096/fasebj.9.2.7781919) / FASEB J. by W Kabsch (1995)
  2. Pollard, T. D. & Cooper, J. A. Actin, a central player in cell shape and movement. Science 326, 1208–1212 (2009). (10.1126/science.1175862) / Science by TD Pollard (2009)
  3. Håkansson, S., Morisaki, H., Heuser, J. E. & Sibley, L. D. Time-lapse video microscopy of gliding motility in Toxoplasma gondii reveals a novel, biphasic mechanism of cell locomotion. Mol. Biol. Cell 10, 3539–3547 (1999). (10.1091/mbc.10.11.3539) / Mol. Biol. Cell by S Håkansson (1999)
  4. Munter, S. et al. Plasmodium sporozoite motility is modulated by the turnover of discrete adhesion sites. Cell Host. Microbe 6, 551–562 (2009). (10.1016/j.chom.2009.11.007) / Cell Host. Microbe by S Munter (2009)
  5. Dobrowolski, J. M. & Sibley, L. D. Toxoplasma invasion of mammalian cells is powered by the actin cytoskeleton of the parasite. Cell 84, 933–939 (1996). (10.1016/S0092-8674(00)81071-5) / Cell by JM Dobrowolski (1996)
  6. Dobrowolski, J. M., Niesman, I. R. & Sibley, L. D. Actin in the parasite Toxoplasma gondii is encoded by a single copy gene, ACT1 and exists primarily in a globular form. Cell Motil. Cytoskeleton 37, 253–262 (1997). (10.1002/(SICI)1097-0169(1997)37:3<253::AID-CM7>3.0.CO;2-7) / Cell Motil. Cytoskeleton by JM Dobrowolski (1997)
  7. Schmitz, S. et al. Malaria parasite actin filaments are very short. J. Mol. Biol. 349, 113–125 (2005). (10.1016/j.jmb.2005.03.056) / J. Mol. Biol. by S Schmitz (2005)
  8. Sahoo, N., Beatty, W. L., Heuser, J. E., Sept, D. & Sibley, L. D. Unusual kinetic and structural properties control rapid assembly and turnover of actin in the parasite Toxoplasma gondii. Mol. Biol. Cell 17, 895–906 (2006). (10.1091/mbc.e05-06-0512) / Mol. Biol. Cell by N Sahoo (2006)
  9. Schmitz, S. et al. Malaria parasite actin polymerisation and filament structure. J. Biol. Chem. 285, 36577–36585 (2010). (10.1074/jbc.M110.142638) / J. Biol. Chem. by S Schmitz (2010)
  10. Schüler, H., Mueller, A. K. & Matuschewski, K. Unusual properties of Plasmodium falciparum actin: new insights into microfilament dynamics of apicomplexan parasites. FEBS Lett. 579, 655–660 (2005). (10.1016/j.febslet.2004.12.037) / FEBS Lett. by H Schüler (2005)
  11. Skillman, K. M. et al. Evolutionarily divergent, unstable filamentous actin is essential for gliding motility of apicomplexan parasites. PLoS Pathog. 7, e1002280 (2011). (10.1371/journal.ppat.1002280) / PLoS Pathog. by KM Skillman (2011)
  12. Pollard, T. D., Blanchoin, L. & Mullins, R. D. Molecular mechanisms controlling actin filament dynamics in nonmuscle cells. Annu. Rev. Biophys. Biomol. Struct. 29, 545–576 (2000). (10.1146/annurev.biophys.29.1.545) / Annu. Rev. Biophys. Biomol. Struct. by TD Pollard (2000)
  13. Nishida, E. & Sakai, H. Kinetic analysis of actin polymerization. J. Biochem. 93, 1011–1020 (1983). (10.1093/oxfordjournals.jbchem.a134224) / J. Biochem. by E Nishida (1983)
  14. Cooper, J. A., Buhle, E. L., Walker, S. B., Tsong, T. Y. & Pollard, T. D. Kinetic evidence for a monomer activation step in actin polymerization. Biochemistry 22, 2193–2202 (1983). (10.1021/bi00278a021) / Biochemistry by JA Cooper (1983)
  15. Miraldi, E. R., Thomas, P. J. & Romberg, L. Allosteric models for cooperative polymerization of linear polymers. Biophys. J. 95, 2470–2486 (2008). (10.1529/biophysj.107.126219) / Biophys. J. by ER Miraldi (2008)
  16. Oosawa, F. & Kasai, M. A theory of linear and helical aggregations of macromolecules. J. Mol. Biol. 4, 10–21 (1962). (10.1016/S0022-2836(62)80112-0) / J. Mol. Biol. by F Oosawa (1962)
  17. Popp, D. & Robinson, R. C. Many ways to build an actin filament. Mol. Micro. 80, 300–308 (2011). (10.1111/j.1365-2958.2011.07599.x) / Mol. Micro. by D Popp (2011)
  18. Frieden, C. Protein aggregation processes: in search of the mechanism. Protein. Sci. 16, 2334–2344 (2007). (10.1110/ps.073164107) / Protein. Sci. by C Frieden (2007)
  19. Cooper, J. A., Walker, S. B. & Pollard, T. D. Pyrene actin: documentation of the validity of a sensitive assay for actin polymerization. J. Muscle. Res. Cell Motil. 4, 253–262 (1983). (10.1007/BF00712034) / J. Muscle. Res. Cell Motil. by JA Cooper (1983)
  20. Pardee, J. D. & Spudich, J. A. Purification of muscle actin. Methods Cell Biol. 24, 271–289 (1982). (10.1016/S0091-679X(08)60661-5) / Methods Cell Biol. by JD Pardee (1982)
  21. Kanzaki, N., Uyeda, T. Q. & Onuma, K. Intermolecular interaction of actin revealed by a dynamic light scattering technique. J. Phys. Chem. B 110, 2881–2887 (2006). (10.1021/jp054865g) / J. Phys. Chem. B by N Kanzaki (2006)
  22. Sept, D. & McCammon, J. A. Thermodynamics and kinetics of actin filament nucleation. Biophys. J. 81, 667–674 (2001). (10.1016/S0006-3495(01)75731-1) / Biophys. J. by D Sept (2001)
  23. Gordon, J. L. & Sibley, L. D. Comparative genome analysis reveals a conserved family of actin-like proteins in apicomplexan parasites. BMC Genomics 6, e179 (2005). (10.1186/1471-2164-6-179) / BMC Genomics by JL Gordon (2005)
  24. Wetzel, D. M., Hakansson, S., Hu, K., Roos, D. & Sibley, L. D. Actin filament polymerization regulates gliding motility by apicomplexan parasites. Mol. Biol. Cell 14, 396–406 (2003). (10.1091/mbc.e02-08-0458) / Mol. Biol. Cell by DM Wetzel (2003)
  25. Mehta, S. & Sibley, L. D. Toxoplasma gondii actin depolymerizing factor acts primarily to sequester G-actin. J. Biol. Chem. 285, 6835–6847 (2010). (10.1074/jbc.M109.068155) / J. Biol. Chem. by S Mehta (2010)
  26. Skillman, K. M., Daher, W., Ma, C. I., Soldati-Favre, D. & Sibley, L. D. Toxoplasma gondii profilin acts primarily to sequester G-actin while formins initiate actin filament formation in vitro. Biochemistry 51, 2486–2495 (2012). (10.1021/bi201704y) / Biochemistry by KM Skillman (2012)
  27. Mehta, S. & Sibley, L. D. Actin depolymerizing factor controls actin turnover and gliding motility in Toxoplasma gondii. Mol. Biol. Cell 22, 1290–1299 (2011). (10.1091/mbc.e10-12-0939) / Mol. Biol. Cell by S Mehta (2011)
  28. Plattner, F. et al. Toxoplasma profilin is essential for host cell invasion and TLR11-dependent induction of an interleukin-12 response. Cell Host Microbe. 3, 77–87 (2008). (10.1016/j.chom.2008.01.001) / Cell Host Microbe. by F Plattner (2008)
  29. Pollard, T. D. & Borisy, G. G. Cellular motility driven by assembly and disassembly of actin filaments. Cell 112, 453–465 (2003). (10.1016/S0092-8674(03)00120-X) / Cell by TD Pollard (2003)
  30. Oda, T., Iwasa, M., Aihara, T., Maeda, Y. & Narita, A. The nature of the globular- to fibrous-actin transition. Nature 457, 441–445 (2009). (10.1038/nature07685) / Nature by T Oda (2009)
  31. Popp, D. et al. Filament structure, organization, and dynamics in MreB sheets. J. Biol. Chem. 285, 15858–15865 (2010). (10.1074/jbc.M109.095901) / J. Biol. Chem. by D Popp (2010)
  32. van den Ent, F., Amos, L. A. & Lowe, J. Prokaryotic origin of the actin cytoskeleton. Nature 413, 39–44 (2001). (10.1038/35092500) / Nature by F van den Ent (2001)
  33. Mayer, J. A. & Amann, K. J. Assembly properties of the Bacillus subtilis actin, MreB. Cell Motil. Cytoskeleton 66, 109–118 (2009). (10.1002/cm.20332) / Cell Motil. Cytoskeleton by JA Mayer (2009)
  34. Gibbon, B. C., Kovar, D. R. & Staiger, C. J. Latrunculin B has different effects on pollen germination and tube growth. Plant Cell 11, 2349–2363 (1999). (10.1105/tpc.11.12.2349) / Plant Cell by BC Gibbon (1999)
  35. Snowman, B. N., Kovar, D. R., Shevchenko, G., Franklin-Tong, V. E. & Staiger, C. J. Signal-mediated depolymerization of actin in pollen during the self-incompatibility response. Plant Cell 14, 2613–2626 (2002). (10.1105/tpc.002998) / Plant Cell by BN Snowman (2002)
  36. De Melo, L. D. et al. Evolutionary conservation of actin-binding proteins in Trypanosoma cruzi and unusual subcellular localization of the actin homologue. Parasitology 135, 955–965 (2008). (10.1017/S0031182008004496) / Parasitology by LD De Melo (2008)
  37. Paredez, A. R. et al. An actin cytoskeleton with evolutionaryly conserved functions in the absence of cannonical actin-binding protiens. PNAS 108, 6151–6156 (2011). (10.1073/pnas.1018593108) / PNAS by AR Paredez (2011)
  38. Sahasrabuddhe, A. A., Bajpai, V. K. & Gupta, C. M. A novel form of actin in Leishmania: molecular characterisation, subcellular localisation and association with subpellicular microtubules. Mol. Biochem. Parasitol. 134, 105–114 (2004). (10.1016/j.molbiopara.2003.11.008) / Mol. Biochem. Parasitol. by AA Sahasrabuddhe (2004)
  39. Humphrey, W., Dalke, A. & Schulten, K. VMD: visual modeling dynamics. Graph 14, 33–38 (1996). (10.1016/0263-7855(96)00018-5) / Graph by W Humphrey (1996)
  40. Heuser, J. E. Procedure for freeze-drying molecules adsorbed to mica flakes. J. Mol. Biol. 169, 155–195 (1983). (10.1016/S0022-2836(83)80179-X) / J. Mol. Biol. by JE Heuser (1983)
  41. Ortega, A., Amoroa, D. & Garcia de la Torre, J. Prediction of hydrodynamic and other solution properties of rigid proteins from atomic and residue-level models. Biophys. J. 101, 892–898 (2011). (10.1016/j.bpj.2011.06.046) / Biophys. J. by A Ortega (2011)
Dates
Type When
Created 12 years ago (Aug. 7, 2013, 5:42 a.m.)
Deposited 2 years, 7 months ago (Jan. 5, 2023, 8:30 p.m.)
Indexed 1 month, 1 week ago (July 20, 2025, 12:31 a.m.)
Issued 12 years ago (Aug. 7, 2013)
Published 12 years ago (Aug. 7, 2013)
Published Online 12 years ago (Aug. 7, 2013)
Funders 0

None

@article{Skillman_2013, title={The unusual dynamics of parasite actin result from isodesmic polymerization}, volume={4}, ISSN={2041-1723}, url={http://dx.doi.org/10.1038/ncomms3285}, DOI={10.1038/ncomms3285}, number={1}, journal={Nature Communications}, publisher={Springer Science and Business Media LLC}, author={Skillman, Kristen M. and Ma, Christopher I. and Fremont, Daved H. and Diraviyam, Karthikeyan and Cooper, John A. and Sept, David and Sibley, L. David}, year={2013}, month=aug }