Protein disulfide isomerase directly interacts with β-actin Cys 374and regulates cytoskeleton reorganization

Journal of Biological Chemistry

Volumn 289, Issue 9, 2014, Pages 5758-5773

  Sobierajska, Katarzyna ^a   Skurzynski, Szymon ^a   Stasiak, Marta ^a   Kryczka, Jakub ^a,b   Cierniewski, Czeslaw S ^a,b   Swiatkowska, Maria ^a  

^a MEDICAL UNIVERSITY OF LODZ   (Poland)

^b INSTITUTE OF MEDICAL BIOLOGY   (Poland)

Author keywords

[No Author keywords available]

Indexed keywords

ANTISENSE OLIGONUCLEOTIDES; EXTRACELLULAR MATRICES; IMMUNOPRECIPITATIONS; PROTEIN DISULFIDE ISOMERASES; SOLID-PHASE BINDING ASSAY; SPECIFIC INTERACTION; SUBCELLULAR COMPARTMENTS; THIOL-DISULFIDE EXCHANGES;

AMINO ACIDS; CELL ADHESION; CELL SIGNALING; CELLS; COVALENT BONDS; EXPERIMENTS;

PROTEINS;

ANTISENSE OLIGONUCLEOTIDE; ARGINYLGLYCYLASPARTIC ACID; BETA ACTIN; CYSTEINE; CYSTEINE 374; FIBRONECTIN; N ETHYLMALEIMIDE; PROTEIN DISULFIDE ISOMERASE; UNCLASSIFIED DRUG;

ARTICLE; CELL ADHESION; CONFOCAL MICROSCOPY; CONTROLLED STUDY; CYTOSKELETON; CYTOSOL; DISULFIDE BOND; DOWN REGULATION; EXTRACELLULAR MATRIX; HUMAN; HUMAN CELL; IMMUNOPRECIPITATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION; SIGNAL TRANSDUCTION; SOLID PHASE SYNTHESIS; SURFACE PLASMON RESONANCE;

ACTIN; ADHESION; CYTOSKELETON; DISULFIDE; THIOL;

ACTINS; ANTINEOPLASTIC AGENTS; CELL ADHESION; CELL LINE; CYTOSKELETON; ENZYME INHIBITORS; ETHYLMALEIMIDE; FIBRONECTINS; HUMANS; OLIGOPEPTIDES; OXIDATION-REDUCTION; PLATELET GLYCOPROTEIN GPIIB-IIIA COMPLEX; PROTEIN DISULFIDE-ISOMERASES; SIGNAL TRANSDUCTION;

EID: 84896865715     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.479477     Document Type: Article

References (33)

1. Hynes, R. O. (1992) Integrins. Versatility, modulation, and signaling in cell adhesion. Cell 69, 11-25
2. Fiaschi, T., Cozzi, G., Raugei, G., Formigli, L., Ramponi, G., and Chiarugi, P. (2006) Redox regulation of β-actin during integrin-mediated cell adhesion. J. Biol. Chem. 281, 22983-22991
3. Stournaras, C. (1990) Exposure of thiol groups and bound nucleotide in G-actin. Thiols as an indicator for the native state of actin. Anticancer Res. 10, 1651-1659
4. 374 regulates actin filament formation by inducing structural changes in the actin molecule. Free Radic. Biol. Med. 34, 23-32
5. 374 mutated human β-actin in two different mammalian cell lines. Impaired microfilament organization and stability. FEBS Lett. 455, 117-122
6. Lassing, I., Schmitzberger, F., Björnstedt, M., Holmgren, A., Nordlund, P., Schutt, C. E., and Lindberg, U. (2007) Molecular and structural basis for redox regulation of β-actin. J. Mol. Biol. 370, 331-348 (Pubitemid 46829216)
7. Hinshaw, D. B., Burger, J. M., Beals, T. F., Armstrong, B. C., and Hyslop P. A. (1991) Actin polymerization in cellular oxidant injury. Arch. Biochem. Biophys. 288, 311-316
8. 2-induced increased in cellular F-actin occur without increases in actin nucleation activity. Arch. Biochem. Biophys. 308, 407-412
9. Gilbert, H. F. (1990) Molecular and cellular aspects of thiol-disulfide exchange. Adv. Enzymol. Relat. Areas Mol. Biol. 63, 69-172
10. López-Mirabal, H. R., and Winther, J. R. (2008) Redox characteristics of the eukaryotic cytosol. Biochim. Biophys. Acta 1783, 629-640
11. Noiva, R. (1999) Protein disulfide isomerase. The multifunctional redox chaperone of endoplasmic reticulum. Semin. Cell Dev. Biol. 10, 481-493
12. Laurindo, F. R., Pescatore, L. A., and de Castro Fernandes, D. (2012) Protein disulfide isomerase in redox cell signaling and homeostasis. Free Radic. Biol. Med. 52, 1954-1969
13. Essex, D. W., and Li, M. (2003) Redox control of platelet aggregation. Biochemistry 42, 129-136 (Pubitemid 36083859)
14. Jasuja, R., Furie, B., and Furie, B. C. (2010) Endothelium-derived but not platelet-derived protein disulfide isomerase is required for thrombus formation in vivo. Blood 116, 4665-4674
15. Essex, D. W., Chen, K., and Swiatkowska, M. (1995) Localization of protein disulfide isomerase to the external surface of the platelet plasma membrane. Blood 86, 2168-2173
16. Swiatkowska, M., Szymański, J., Padula, G., and Cierniewski, C. S. (2008) Interaction and functional association of protein disulfide isomerase with αVβ3 integrin on endothelial cells. FEBS J. 275, 1813-1823 (Pubitemid 351464001)
17. Farwell, A. P., Lynch, R. M., Okulicz, W. C., Comi, A. M., and Leonard, J. L. (1990) The actin cytoskeleton mediates the hormonally regulated translocation of type II Iodothyronine 5′-Deiodinase in astrocytes. J. Biol. Chem. 265, 18546-18553
18. Safran, M., Farwell, A. P., and Leonard, J. L. (1992) Thyroid hormone-dependent redistribution of the 55-kilodalton monomer of protein disulfide isomerase in cultured glial cells. Endocrinology 131, 2413-2418
19. Ogura, M., Morishima, Y., Ohno, R., Kato, Y., Hirabayashi, N., Nagura, H., and Saito, H. (1985) Establishment of a novel human megakaryoblastic leukemia cell line, MEG-01, with positive Philadelphia chromosome. Blood 66, 1384-1392 (Pubitemid 16194703)
20. Zai, A., Rudd, M. A., Scribner, A. W., and Loscalzo, J. (1999) Cell-surface protein disulfide isomerase catalyzes transnitrosation and regulates intracellular transfer of nitric oxide. J. Clin. Invest. 103, 393-399 (Pubitemid 29069989)
21. Thepparit, C., and Smith, D. R. (2004) Serotype-specific entry of dengue virus into liver cells. Identification of the 37-kilodalton/67-kilodalton high-affinity laminin receptor as a dengue virus serotype 1 receptor. J. Virol. 78, 12647-12656 (Pubitemid 39458782)
22. Towbin, H., Staehelin, T., and Gordon, J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets. Procedure and some applications. Proc. Natl. Acad. Sci. U.S.A. 76, 4350-4354 (Pubitemid 9256559)
23. Dugina, V., Zwaenepoel, I., Gabbiani, G., Clément, S., and Chaponnier, C. (2009) β- and γ-cytoplasmic actins display distint distribution and function diversity. J. Cell Sci. 122, 2980-2988
24. Dalle-Donne, I., Giustarini, D., Colombo, R., Milzani, A., and Rossi, R. (2005) S-Glutathionylation in human platelets by a thiol-disulfide exchange-independent mechanism. Free Radic. Biol. Med. 38, 1501-1510 (Pubitemid 40693834)
25. Wang, J., Boja, E. S., Tan, W., Tekle, E., Fales, H. M., English, S., Mieyal, J. J., and Chock, P. B. (2001) Reversible glutathionylation regulates actin polymerization in A431 cells. J. Biol. Chem. 276, 47763-47766
26. Dalle-Donne, I., Milzani, A., Gagliano, N., Colombo, R., Giustarini, D., and Rossi, R. (2008) Molecular mechanisms and potential clinical significance of S-glutathionylation. Antioxid. Redox Signal. 10, 445-473
27. Reinhardt, C., von Brühl, M. L., Manukyan, D., Grahl, L., Lorenz, M., Altmann, B., Dlugai, S., Hess, S., Konrad, I., Orschiedt, L., Mackman, N., Ruddock, L., Massberg, S., and Engelmann, B. (2008) Protein disulfide isomerase acts as an injury response signal that enhances fibrin generation via tissue factor activation. J. Clin. Invest. 118, 1110-1122 (Pubitemid 351364618)
28. Peltoniemi, M. J., Karala, A. R., Jurvansuu, J. K., Kinnula, V. L., and Ruddock, L. W. (2006) Insights into deglutathionylation reactions. Different intermediates in the glutaredoxin and protein disulfide isomerase catalyzed reactions are defined by the gamma-linkage present in glutathione. J. Biol. Chem. 281, 33107-33114 (Pubitemid 46036692)
29. Ruoppolo, M., and Freedman, R. B. (1995) Refolding by disulfide isomerization. The mixed disulfide between ribonuclease T1 and glutathione as a model refolding substrate. Biochemistry 34, 9380-9388
30. Ruoppolo, M., Freedman, R. B., Pucci, P., and Marino, G. (1996) Glutathione-dependent pathways of refolding of RNase T1 by oxidation and disulfide isomerization. Catalysis by protein disulfide isomerase. Biochemistry 35, 13636-13646 (Pubitemid 26359176)
31. Paes, A. M., Veríssimo-Filho, S., Guimarães, L. L., Silva, A. C., Takiuti, J. T., Santos, C. X., Janiszewski, M., Laurindo, F. R., and Lopes, L. R. (2011) Protein disulfide isomerase redox-dependent association with p47 (phox). Evidence for an organizer role in leukocyte NADPH oxidase activation. J. Leukocyte Biol. 90, 799-810
32. Chiarugi, P., and Fiaschi, T. (2007) Redox signaling in anchorage-dependent cell growth. Cell. Signal. 19, 672-682 (Pubitemid 46275378)
33. Tang, J. X., Janmey, P. A., Stossel, T. P., and Ito, T. (1999) Thiol oxidation of actin produces dimmers that enhance the elasticity of the F-actin network. Biophys. J. 76, 2208-2215 (Pubitemid 29266374)