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dc.contributor.author
Burgardt, Noelia Ines
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dc.contributor.author
Schmidt, Andreas
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dc.contributor.author
Manns, Annika
dc.contributor.author
Schutkowski, Alexandra
dc.contributor.author
Jahreis, Günther
dc.contributor.author
Lin, Yi Jan
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dc.contributor.author
Schulze, Bianca
dc.contributor.author
Masch, Antonia
dc.contributor.author
Lücke, Christian
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dc.contributor.author
Weiwad, Matthias
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dc.date.available
2018-12-27T17:22:45Z
dc.date.issued
2015-07
dc.identifier.citation
Burgardt, Noelia Ines; Schmidt, Andreas; Manns, Annika; Schutkowski, Alexandra; Jahreis, Günther; et al.; Parvulin 17-catalyzed tubulin polymerization is regulated by calmodulin in a calcium-dependent manner; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 290; 27; 7-2015; 16708-16722
dc.identifier.issn
0021-9258
dc.identifier.uri
http://hdl.handle.net/11336/67072
dc.description.abstract
Recently we have shown that the peptidyl-prolyl cis/trans isomerase parvulin 17 (Par17) interacts with tubulin in a GTPdependent manner, thereby promoting the formation of microtubules. Microtubule assembly is regulated by Ca2+-loaded calmodulin (Ca2+/CaM) both in the intact cell and under in vitro conditions via direct interaction with microtubule-associated proteins. Here we provide the first evidence that Ca2+/CaM interacts also with Par17 in a physiologically relevant way, thus preventing Par17-promoted microtubule assembly. In contrast, parvulin 14 (Par14), which lacks only the first 25 N-terminal residues of the Par17 sequence, does not interact with Ca2+/CaM, indicating that this interaction is exclusive for Par17. Pulldown experiments and chemical shift perturbation analysis with 15N-labeled Par17 furthermore confirmed that calmodulin (CaM) interacts in a Ca2+-dependent manner with the Par17 N terminus. The reverse experiment with 15N-labeled Ca2+/CaM demonstrated that the N-terminal Par17 segment binds to both CaM lobes simultaneously, indicating that Ca2+/CaM undergoes a conformational change to form a binding channel between its two lobes, apparently similar to the structure of the CaM-smMLCK796-815 complex. In vitro tubulin polymerization assays furthermore showed that Ca2+/CaM completely suppresses Par17-promoted microtubule assembly. The results imply that Ca2+/CaM binding to the N-terminal segment of Par17 causes steric hindrance of the Par17 active site, thus interfering with the Par17/tubulin interaction. This Ca2+/CaM-mediated control of Par17-assisted microtubule assembly may provide a mechanism that couples Ca2+ signaling with microtubule function.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
American Society for Biochemistry and Molecular Biology
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dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Nuclear Magnetic Resonance
dc.subject
Protein-Protein Interaction
dc.subject
Parvulin
dc.subject
Calmodulin
dc.subject.classification
Otras Ciencias Biológicas
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dc.subject.classification
Ciencias Biológicas
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dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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dc.title
Parvulin 17-catalyzed tubulin polymerization is regulated by calmodulin in a calcium-dependent manner
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2018-09-11T14:52:08Z
dc.journal.volume
290
dc.journal.number
27
dc.journal.pagination
16708-16722
dc.journal.pais
Estados Unidos
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dc.journal.ciudad
Bethesda
dc.description.fil
Fil: Burgardt, Noelia Ines. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Max Planck Research Unit for Enzymology of Protein Folding; Alemania
dc.description.fil
Fil: Schmidt, Andreas. Max Planck Research Unit for Enzymology of Protein Folding; Alemania
dc.description.fil
Fil: Manns, Annika. Max Planck Research Unit for Enzymology of Protein Folding; Alemania
dc.description.fil
Fil: Schutkowski, Alexandra. Max Planck Research Unit for Enzymology of Protein Folding; Alemania
dc.description.fil
Fil: Jahreis, Günther. Max Planck Research Unit for Enzymology of Protein Folding; Alemania
dc.description.fil
Fil: Lin, Yi Jan. Kaohsiung Medical University; Alemania
dc.description.fil
Fil: Schulze, Bianca. Max Planck Research Unit for Enzymology of Protein Folding; Alemania
dc.description.fil
Fil: Masch, Antonia. Martin Luther University Halle Wittenberg; Alemania
dc.description.fil
Fil: Lücke, Christian. Max Planck Research Unit for Enzymology of Protein Folding; Alemania
dc.description.fil
Fil: Weiwad, Matthias. Max Planck Research Unit for Enzymology of Protein Folding; Alemania. Martin Luther University Halle Wittenberg; Alemania
dc.journal.title
Journal of Biological Chemistry (online)
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://www.jbc.org/content/290/27/16708
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/https://dx.doi.org/10.1074/jbc.M114.593228
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