Registro completo de metadatos
| Campo DC | Valor | Lengua/Idioma |
|---|---|---|
| dc.creator | Burgardt, Noelia Ines | - |
| dc.creator | Schmidt, Andreas | - |
| dc.creator | Manns, Annika | - |
| dc.creator | Schutkowski, Alexandra | - |
| dc.creator | Jahreis, Günther | - |
| dc.creator | Lin, Yi Jan | - |
| dc.creator | Schulze, Bianca | - |
| dc.creator | Masch, Antonia | - |
| dc.creator | Lücke, Christian | - |
| dc.creator | Weiwad, Matthias | - |
| dc.date | 2018-12-27T17:22:45Z | - |
| dc.date | 2018-12-27T17:22:45Z | - |
| dc.date | 2015-07 | - |
| dc.date | 2018-09-11T14:52:08Z | - |
| dc.date.accessioned | 2019-04-29T15:42:16Z | - |
| dc.date.available | 2019-04-29T15:42:16Z | - |
| dc.date.issued | 2015-07 | - |
| dc.identifier | 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 | 0021-9258 | - |
| dc.identifier | http://hdl.handle.net/11336/67072 | - |
| dc.identifier | CONICET Digital | - |
| dc.identifier | CONICET | - |
| dc.identifier.uri | http://rodna.bn.gov.ar:8080/jspui/handle/bnmm/299976 | - |
| dc.description | 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.description | 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: Schmidt, Andreas. Max Planck Research Unit for Enzymology of Protein Folding; Alemania | - |
| dc.description | Fil: Manns, Annika. Max Planck Research Unit for Enzymology of Protein Folding; Alemania | - |
| dc.description | Fil: Schutkowski, Alexandra. Max Planck Research Unit for Enzymology of Protein Folding; Alemania | - |
| dc.description | Fil: Jahreis, Günther. Max Planck Research Unit for Enzymology of Protein Folding; Alemania | - |
| dc.description | Fil: Lin, Yi Jan. Kaohsiung Medical University; Alemania | - |
| dc.description | Fil: Schulze, Bianca. Max Planck Research Unit for Enzymology of Protein Folding; Alemania | - |
| dc.description | Fil: Masch, Antonia. Martin Luther University Halle Wittenberg; Alemania | - |
| dc.description | Fil: Lücke, Christian. Max Planck Research Unit for Enzymology of Protein Folding; Alemania | - |
| dc.description | Fil: Weiwad, Matthias. Max Planck Research Unit for Enzymology of Protein Folding; Alemania. Martin Luther University Halle Wittenberg; Alemania | - |
| dc.format | application/pdf | - |
| dc.format | application/pdf | - |
| dc.language | eng | - |
| dc.publisher | American Society for Biochemistry and Molecular Biology | - |
| dc.relation | info:eu-repo/semantics/altIdentifier/url/http://www.jbc.org/content/290/27/16708 | - |
| dc.relation | info:eu-repo/semantics/altIdentifier/doi/https://dx.doi.org/10.1074/jbc.M114.593228 | - |
| dc.rights | info:eu-repo/semantics/openAccess | - |
| dc.rights | https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ | - |
| dc.source | reponame:CONICET Digital (CONICET) | - |
| dc.source | instname:Consejo Nacional de Investigaciones Científicas y Técnicas | - |
| dc.source | instacron:CONICET | - |
| dc.subject | NUCLEAR MAGNETIC RESONANCE | - |
| dc.subject | PROTEIN-PROTEIN INTERACTION | - |
| dc.subject | PARVULIN | - |
| dc.subject | CALMODULIN | - |
| dc.subject | Otras Ciencias Biológicas | - |
| dc.subject | Ciencias Biológicas | - |
| dc.subject | CIENCIAS NATURALES Y EXACTAS | - |
| 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:eu-repo/semantics/publishedVersion | - |
| dc.type | info:ar-repo/semantics/articulo | - |
| Aparece en las colecciones: | CONICET | |
Ficheros en este ítem:
No hay ficheros asociados a este ítem.