Mapping of Drebrin Binding Site on F-Actin

Journal of Molecular Biology

Volumn 398, Issue 4, 2010, Pages 542-554

  Grintsevich, Elena E ^a   Galkin, Vitold E ^b   Orlova, Albina ^b   Ytterberg, A Jimmy ^a,d   Mikati, Mouna M ^a   Kudryashov, Dmitri S ^a   Loo, Joseph A ^a,c   Egelman, Edward H ^b   Reisler, Emil ^a,c  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF VIRGINIA   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

^d UNIVERSITY OF SOUTHERN DENMARK   (Denmark)

Author keywords

Actin; Cross linking; Drebrin; Electron microscopy; Mass spectrometry

Indexed keywords

DREBRIN; F ACTIN; RECOMBINANT PROTEIN; ACTIN; CROSS LINKING REAGENT; DREBRINS; NEUROPEPTIDE;

ACTIN FILAMENT; AMINO TERMINAL SEQUENCE; ANIMAL TISSUE; ARTICLE; BINDING SITE; CONTROLLED STUDY; ELECTRON MICROSCOPY; GENE CONSTRUCT; GENE INTERACTION; GENE MAPPING; GENETIC POLYMORPHISM; MASS SPECTROMETRY; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN CROSS LINKING; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; SITE DIRECTED MUTAGENESIS; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; CHEMICAL STRUCTURE; GENETICS; METABOLISM; MOLECULAR GENETICS; PROTEIN ANALYSIS; PROTEIN BINDING;

ACTINS; AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; BINDING SITES; CROSS-LINKING REAGENTS; MASS SPECTROMETRY; MICROSCOPY, ELECTRON; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; NEUROPEPTIDES; PROTEIN BINDING; PROTEIN INTERACTION MAPPING;

EID: 77951905040     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.03.039     Document Type: Article

References (44)

1. Sekino Y., Kojima N., Shirao T. Role of actin cytoskeleton in dendritic spine morphogenesis. Neurochem. Int. 2007, 51:92-104.
2. Kojima N., Shirao T. Synaptic dysfunction and disruption of postsynaptic drebrin-actin complex: a study of neurological disorders accompanied by cognitive deficits. Neurosci. Res. 2007, 58:1-5.
3. Peitsch W.K., Hofmann I., Pratzel S., Grund C., Kuhn C., Moll I, et al. Drebrin particles: components in the ensemble of proteins regulating actin dynamics of lamellipodia and filopodia. Eur. J. Cell Biol. 2001, 80:567-579.
4. Peitsch W.K., Hofmann I., Endlich N., Pratzel S., Kuhn C., Spring H., et al. Cell biological and biochemical characterization of drebrin complexes in mesangial cells and podocytes of renal glomeruli. J. Am. Soc. Nephrol. 2003, 14:1452-1463.
5. Grenklo S., Hillberg L., Zhao Rathje L.S., Pinaev G., Schutt C., Lindberg U. Tropomyosin assembly intermediates in the control of microfilament system turnover. Eur. J. Cell Biol. 2008, 87:905-920.
6. Ishikawa R., Hayashi K., Shirao T., Xue Y., Takagi T., Sasaki Y., Kohama K. Drebrin, a development-associated brain protein from rat embryo, causes the dissociation of tropomyosin from actin filaments. J. Biol. Chem. 1994, 269:29928-29933.
7. Sasaki Y., Hayashi K., Shirao T., Ishikawa R., Kohama K. Inhibition by drebrin of the actin-bundling activity of brain fascin, a protein localized in filopodia of growth cones. J. Neurochem. 1996, 66:980-988.
8. Biou V., Brinkhaus H., Malenka R.C., Matus A. Interactions between drebrin and Ras regulate dendritic spine plasticity. Eur. J. Neurosci. 2008, 27:2847-2859.
9. Hayashi K., Ishikawa R., Ye L.H., He X.L., Takata K., Kohama K., Shirao T. Modulatory role of drebrin on the cytoskeleton within dendritic spines in the rat cerebral cortex. J. Neurosci. 1996, 16:7161-7170.
10. Ishikawa R., Katoh K., Takahashi A., Xie C., Oseki K., Watanabe M., et al. Drebrin attenuates the interaction between actin and myosin-V. Biochem. Biophys. Res. Commun. 2007, 359:398-401.
11. Zhao L., Ma Q.L., Calon F., Harris-White M.E., Yang F., Lim G.P., et al. Role of p21-activated kinase pathway defects in the cognitive deficits of Alzheimer disease. Nat. Neurosci. 2006, 9:234-242.
12. Kessels M.M., Engqvist-Goldstein A.E.Y., Drubin D.G. Association of mouse actin-binding protein 1 (mAbp1/SH3P7), an Src kinase target, with dynamic regions of the cortical actin cytoskeleton in response to Rac1 activation. Mol. Biol. Cell 2000, 11:393-412.
13. Xu W., Stamnes M. The actin-depolymerizing factor homology and charged/helical domains of drebrin and mAbp1 direct membrane binding and localization via distinct interactions with actin. J. Biol. Chem. 2006, 281:11826-11833.
14. Hayashi K., Ishikawa R., Kawai-Hirai R., Takagi T., Taketomi A., Shirao T. Domain analysis of the actin-binding and actin-remodeling activities of drebrin. Exp. Cell Res. 1999, 253:673-680.
15. Hayashi K., Shirao T. Change in the shape of dendritic spines caused by overexpression of drebrin in cultured cortical neurons. J. Neurosci. 1999, 19:3918-3925.
16. Haeckel A., Ahuja R., Gundelfinger E.D., Qualmann B., Kessels M.M. The actin-binding protein Abp1 controls dendritic spine morphology and is important for spine head and synapse formation. J. Neurosci. 2008, 28:10031-10044.
17. Galkin V.E., Orlova A., Lukoyanova N., Wriggers W., Egelman E.H. Actin depolymerizing factor stabilizes an existing state of F-actin and can change the tilt of F-actin subunits. J. Cell Biol. 2001, 153:75-86.
18. Reichert A., Heintz D., Echner H., Voelter W., Faulstich H. Identification of contact sites in the actin-thymosin beta4 complex by distance-dependent thiol cross-linking. J. Biol. Chem. 1996, 271:1301-1308.
19. Kim E., Miller C., Reisler E. Polymerization and in vitro motility properties of yeast actin: a comparison with rabbit skeletal α-actin. Biochemistry 1996, 35:16566-16572.
20. Gerson J.H., Kim E., Muhlrad A., Reisler E. Tropomyosin-troponin regulation of actin does not involve subdomain 2 motions. J. Biol. Chem. 2001, 276:18442-18449.
21. Grintsevich E.E., Benchaar S.A., Warshaviak D., Boontheung P., Halgand F., Whitelegge J.P., et al. Mapping the cofilin binding site on yeast G-actin by chemical cross-linking. J. Mol. Biol. 2008, 377:395-409.
22. Cole C., Barber J.D., Barton G.J. The Jpred 3 secondary structure prediction server. Nucleic Acids Res. 2008, 36:W197-W201.
23. Holmes K.C., Popp D., Gebhard W., Kabsch W. Atomic model of the actin filament. Nature 1990, 347:44-49.
24. McGough A., Way M., DeRosier D. Determination of the alpha-actinin-binding site on actin filaments by cryoelectron microscopy and image analysis. J. Cell Biol. 1994, 126:433-443.
25. Egelman E.H. A robust algorithm for the reconstruction of helical filaments using single-particle methods. Ultramicroscopy 2000, 85:225-234.
26. Galkin V.E., Orlova A., VanLoock M.S., Rybakova I.N., Ervasti J.M., Egelman E.H. The utrophin actin-binding domain binds F-actin in two different modes: implications for the spectrin superfamily of proteins. J. Cell Biol. 2002, 157:243-251.
27. Lehman W., Galinska-Rakoczy A., Hatch V., Tobacman L.S., Craig R. Structural basis for the activation of muscle contraction by troponin and tropomyosin. J. Mol. Biol. 2009, 388:673-681.
28. Bacchiocchi C., Graceffa P., Lehrer S.S. Myosin-induced movement of [alpha][alpha], [alpha][beta], and [beta][beta] smooth muscle tropomyosin on actin observed by multisite FRET. Biophys. J. 2004, 86:2295-2307.
29. 2+-induced tropomyosin movement in Limulus thin filaments revealed by three-dimensional reconstruction. Nature 1994, 368:65-67.
30. Xu C., Craig R., Tobacman L., Hororwitz R., Lehman W. Tropomyosin positions in regulated thin filaments revealed by cryoelectron microscopy. Biophys. J. 1999, 77:985-992.
31. McGough A., Pope B., Chiu W., Weeds A. Cofilin changes the twist of F-actin: implications for actin filament dynamics and cellular function. J. Cell Biol. 1997, 138:771-781.
32. Paavilainen V.O., Oksanen E., Goldman A., Lappalainen P. Structure of the actin-depolymerizing factor homology domain in complex with actin. J. Cell Biol. 2008, 182:51-59.
33. Wyszynski M., Lin J., Rao A., Nigh E., Beggs A.H., Craig A.M., Sheng M. Competitive binding of [alpha]-actinin and calmodulin to the NMDA receptor. Nature 1997, 385:439-442.
34. Shirao T., Sekino Y. Clustering and anchoring mechanisms of molecular constituents of postsynaptic scaffolds in dendritic spines. Neurosci. Res. 2001, 40:1-7.
35. Holmes K.C., Angert I., Jon Kull F., Jahn W., Schroder R.R. Electron cryo-microscopy shows how strong binding of myosin to actin releases nucleotide. Nature 2003, 425:423-427.
36. Spudich J.A., Watt S. 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. 1971, 246:4866-4871.
37. Shevchenko A., Wilm M., Vorm O., Mann M. Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels. Anal. Chem. 1996, 68:850-858.
38. Ytterberg A.J., Peltier J.B., van Wijk K.J. Protein profiling of plastoglobules in chloroplasts and chromoplasts. A surprising site for differential accumulation of metabolic enzymes. Plant Physiol. 2006, 140:984-997.
39. Gobom J., Nordhoff E., Mirgorodskaya E., Ekman R., Roepstorff P. Sample purification and preparation technique based on nano-scale reversed-phase columns for the sensitive analysis of complex peptide mixtures by matrix-assisted laser desorption/ionization mass spectrometry. J. Mass Spectrom. 1999, 34:105-116.
40. Frank J., Shimkin B., Dowse H. Spider-a modular software system for electron image processing. Ultramicroscopy 1981, 6:343-357.
41. Ludtke S.J., Baldwin P.R., Chiu W. EMAN: semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 1999, 128:82-97.
42. Galkin V.E., Orlova A., Lukoyanova N., VanLoock M.S., Haag P., Bullard B., Egelman E.H. The location of ubiquitin in Lethocerus arthrin. J. Mol. Biol. 2003, 325:623-628.
43. Pettersen E.E., Goddard T.D., Huang C.C., Couch G.S., Greenblatt D.M., Meng E.C., Ferrin T.E. UCSF Chimera-visualization system for exploratory research and analysis. J. Comput. Chem. 2004, 25:1605-1612.
44. Schutt C.E., Myslik J.C., Rozycki M.D., Goonesekere N.C.W., Lindberg U. The structure of crystalline profilin-[beta]-actin. Nature 1993, 365:810-816.