Identification of Novel Interaction between ADAM17 (a Disintegrin and Metalloprotease 17) and Thioredoxin-1

Aragão, Annelize Zambon Barbosa; Nogueira, Maria Luiza Caldas; Granato, Daniela Campos; Simabuco, Fernando Moreira; Honorato, Rodrigo Vargas; Hoffman, Zaira; Yokoo, Sami; Laurindo, Francisco Rafael Martins; Squina, Fábio M.; Zeri, Ana Carolina de Mattos; Oliveira, Paulo Sérgio Lopes de; Sherman, Nicholas E.; Leme, Adriana Franco Paes

doi:10.1074/jbc.m112.364513

Cited by 37 publications

(52 citation statements)

References 50 publications

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“…Cross-linking reactions were performed as described in Aragão et al (2012) [24]. In summary, 5 x 10 -10 mol of each purified recombinant protein was incubated with 1.25 mM disuccinimidyl suberate (DSS, spacer arm length: 11.4 Å, Sigma-Aldrich) for 2 h at room temperature, followed by quenching with Laemmli sample buffer.…”

Section: Methodsmentioning

confidence: 99%

Structural Analysis of Intermolecular Interactions in the Kinesin Adaptor Complex Fasciculation and Elongation Protein Zeta 1/ Short Coiled-Coil Protein (FEZ1/SCOCO)

et al. 2013

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Cytoskeleton and protein trafficking processes, including vesicle transport to synapses, are key processes in neuronal differentiation and axon outgrowth. The human protein FEZ1 (fasciculation and elongation protein zeta 1 / UNC-76, in C. elegans), SCOCO (short coiled-coil protein / UNC-69) and kinesins (e.g. kinesin heavy chain / UNC116) are involved in these processes. Exploiting the feature of FEZ1 protein as a bivalent adapter of transport mediated by kinesins and FEZ1 protein interaction with SCOCO (proteins involved in the same path of axonal growth), we investigated the structural aspects of intermolecular interactions involved in this complex formation by NMR (Nuclear Magnetic Resonance), cross-linking coupled with mass spectrometry (MS), SAXS (Small Angle X-ray Scattering) and molecular modelling. The topology of homodimerization was accessed through NMR (Nuclear Magnetic Resonance) studies of the region involved in this process, corresponding to FEZ1 (92-194). Through studies involving the protein in its monomeric configuration (reduced) and dimeric state, we propose that homodimerization occurs with FEZ1 chains oriented in an anti-parallel topology. We demonstrate that the interaction interface of FEZ1 and SCOCO defined by MS and computational modelling is in accordance with that previously demonstrated for UNC-76 and UNC-69. SAXS and literature data support a heterotetrameric complex model. These data provide details about the interaction interfaces probably involved in the transport machinery assembly and open perspectives to understand and interfere in this assembly and its involvement in neuronal differentiation and axon outgrowth.

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Section: Methodsmentioning

confidence: 99%

Structural Analysis of Intermolecular Interactions in the Kinesin Adaptor Complex Fasciculation and Elongation Protein Zeta 1/ Short Coiled-Coil Protein (FEZ1/SCOCO)

et al. 2013

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“…In order to validate one of the proteins identified by LC-MS/ MS analysis, an independent experiment was carried out to perform an immunoblotting against S100-A9 calcium-binding protein as described before [Aragão et al, 2012b]. The proteins extracted from all treatment groups were separated by 4-15% SDS-PAGE and transferred onto nitrocellulose membrane (GE Healthcare) by semidry system (Bio-Rad).…”

Section: Immunoblottingmentioning

confidence: 99%

Acidulated Phosphate Fluoride Application Changes the Protein Composition of Human Acquired Enamel Pellicle

et al. 2013

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We evaluated, by proteomic analysis, whether the chemical changes provoked on enamel by acidulated phosphate fluoride (APF) application alter the protein composition of acquired enamel pellicle. Enamel slabs, pretreated with distilled water (negative control), phosphoric acid (active control) or APF solution, were immersed in human saliva for pellicle formation. The adsorbed proteins were extracted and analyzed by liquid chromatography-mass spectrometry/mass spectrometry. Fifty-six proteins were identified, 12 exclusive to APF and 11 to phosphoric acid. APF decreased the concentration of histatin-1, but increased the concentration of S100-A9, which is confirmed by immunoblotting. The findings suggest that APF application changes the acquired enamel pellicle composition.

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“…For cross-linking analysis, the raw data files generated by Xcalibur v.2.1 (Thermo Fisher Scientific) were converted to a peak list format (mgf) using Proteome Discoverer version 1. Computational Biology-To obtain a model of the glutaminase fiber, we applied a previously developed rigid body docking algorithm restrained by experimental DSS cross-linking data (20). Initially, we reconstructed both the N-and C-terminal regions of the monomers using a loop reconstruction routine and placed a copy of the tetramer, namely the ligand domain, on the N-terminal of the receptor domain.…”

Section: Cross-linking Analysis Of Gac Complexes By Lc-ms/ms-mentioning

confidence: 99%

Active Glutaminase C Self-assembles into a Supratetrameric Oligomer That Can Be Disrupted by an Allosteric Inhibitor

Ferreira

Cassago

Gonçalves

et al. 2013

Journal of Biological Chemistry

125

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Background: GAC supplies for increased metabolic needs of tumors because of exclusive localization and kinetic properties. Results: Higher than tetramer oligomers are the active form in in vitro and in cellular assays. Bis-2-(5-phenylacetamido-1,3,4-thiadiazol-2-yl)ethyl sulfide disrupts oligomers. Conclusion: A novel molecular mechanism for GAC activation is proposed. Significance: The data affect the development of therapies targeting GAC in tumors, with emphasis on allosteric inhibitors.

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Identification of Novel Interaction between ADAM17 (a Disintegrin and Metalloprotease 17) and Thioredoxin-1

Cited by 37 publications

References 50 publications

Structural Analysis of Intermolecular Interactions in the Kinesin Adaptor Complex Fasciculation and Elongation Protein Zeta 1/ Short Coiled-Coil Protein (FEZ1/SCOCO)

Structural Analysis of Intermolecular Interactions in the Kinesin Adaptor Complex Fasciculation and Elongation Protein Zeta 1/ Short Coiled-Coil Protein (FEZ1/SCOCO)

Acidulated Phosphate Fluoride Application Changes the Protein Composition of Human Acquired Enamel Pellicle

Active Glutaminase C Self-assembles into a Supratetrameric Oligomer That Can Be Disrupted by an Allosteric Inhibitor

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