Molecular and Structural Basis for Redox Regulation of β-Actin

Lassing, Ingrid; Schmitzberger, F.; Björnstedt, Mikael; Holmgren, Arne; Nordlund, P.; Schutt, Clarence E.; Lindberg, Uno

doi:10.1016/j.jmb.2007.04.056

Cited by 140 publications

(122 citation statements)

References 107 publications

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“…On the other hand, reactive oxygen species are known to interfere with the organization of actin microfilaments and motility of many eukaryotic cells (32). Therefore, oxidation of Cys 374 could be critical for the disassembly of filaments, when the environment is more oxidative because of a shifted GSH/ GSSH equilibrium (6). The formation of disulfide bonds between ␤-actin monomers may be fundamental during cellular redox responses to growth factors or integrin stimulation.…”

Section: Discussionmentioning

confidence: 99%

“…The glutathionylation of ␤-actin that occurs during cell adhesion leads to the disassembly of actomyosin filaments (2). On the other hand, oxidation of ␤-actin creates intermolecular disulfide bonds between Cys 374 residues of neighboring ␤-actin molecules and thus prevents ␤-actin polymerization (6). In consequence, it leads to a cytoskeleton rearrangement (7,8).…”

mentioning

confidence: 99%

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Protein Disulfide Isomerase Directly Interacts with β-Actin Cys374 and Regulates Cytoskeleton Reorganization

Sobierajska

Skurzynski

Stasiak

et al. 2014

Journal of Biological Chemistry

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Background: PDI regulates cytoskeleton reorganization by the thiol-disulfide exchange in ␤-actin. Results: PDI directly binds to Cys 374 of ␤-actin during cell adhesion and spreading. Conclusion: Interaction of PDI with ␤-actin is induced by integrin-mediated cell adhesion and promotes cytoskeleton reorganization. Significance: PDI is a new regulator of the intramolecular disulfide-thiol rearrangement of ␤-actin in response to ␣IIb␤3 integrin engagement.

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Protein Disulfide Isomerase Directly Interacts with β-Actin Cys374 and Regulates Cytoskeleton Reorganization

Sobierajska

Skurzynski

Stasiak

et al. 2014

Journal of Biological Chemistry

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“…The implication of actin cysteine residues has been described in the regulation of actin conformational states in which the formation of a sulfinic acid (at C272) and inter-disulphide bridges via C374 play a role (42). Considering ERp57 reductase activity, we evaluated the possible involvement of the cysteine oxidation status of ß-actin in the interaction with ERp57.…”

Section: Disulphide Bonds Modulate ß-Actin Association With Erp57mentioning

confidence: 99%

Characterisation of a multimeric protein complex associated with ERp57 within the nucleus in paclitaxel-sensitive and -resistant epithelial ovarian cancer cells: The involvement of specific conformational states of β-actin

Cicchillitti¹,

Corte

Michele

et al. 2010

Int J Oncol

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Abstract. Ovarian cancer is the second most frequently diagnosed malignancy of the reproductive system and is the leading cause of gynecological cancer mortality. Although the majority of advanced ovarian carcinomas initially respond successfully to taxane-based chemotherapy, resistance to chemotherapy remains the primary factor accounting for the low 5-year survival in this patient population. Recent data obtained by our group demonstrate that the disulphide isomerase ERp57 is strongly modulated in paclitaxel resistance suggesting that it may represent a chemoresistance biomarker in ovarian cancer. In the present study, we characterise a nuclear multimeric complex where ERp57 is associated with protein species involved in cell division and gene expression, as Nucleolin, Nucleophosmin, Vimentin, Aurora kinase C and ß-actin. In particular, we show that the occurrence of the interaction of nuclear ERp57 with ß-actin is associated with paclitaxel resistance and that specific actin conformations modulate this complex. We propose the involvement of the nuclear ERp57 complex in mechanisms associated with chromosome segregation in which specific conformational states of actin play a role in the pathway involved in paclitaxel resistance.

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“…Other targets include transcription factors (41,46), kinases (e.g. Src, (47)), small GTPases (48-52), matrix metalloproteinases (41,53), actin (54,55) and actin-associated molecules (56)(57)(58). ROS acting on these targets will give rise to numerous feedback and feedforward reactions and is likely responsible for providing signal amplification and mediating cross-talk between different signal cascades (59).…”

Section: Integrins and Reactive Oxygen Speciesmentioning

confidence: 99%

Common and Diverging Integrin Signals Downstream of Adhesion and Mechanical Stimuli and Their Interplay with Reactive Oxygen Species

Zeller

Johansson

2014

Biophys. Rev. Lett.

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The integrin family of adhesion receptors regulates basic functions of cells, and the signals they induce are altered in tumor cells. In this review we discuss how different integrin-dependent signals are generated during cell adhesion and by physical forces acting on cells. We also describe how reactive oxygen species are integral parts of integrin signaling and highlight a few important questions in the field. Answers to those may improve our understanding of integrins and their role in the development of cancer.

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Molecular and Structural Basis for Redox Regulation of β-Actin

Cited by 140 publications

References 107 publications

Protein Disulfide Isomerase Directly Interacts with β-Actin Cys374 and Regulates Cytoskeleton Reorganization

Protein Disulfide Isomerase Directly Interacts with β-Actin Cys374 and Regulates Cytoskeleton Reorganization

Characterisation of a multimeric protein complex associated with ERp57 within the nucleus in paclitaxel-sensitive and -resistant epithelial ovarian cancer cells: The involvement of specific conformational states of β-actin

Common and Diverging Integrin Signals Downstream of Adhesion and Mechanical Stimuli and Their Interplay with Reactive Oxygen Species

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