Upload resources

Upload your works to SEDICI to increase its visibility and improve its impact

 

Show simple item record

dc.date.accessioned 2019-12-20T18:17:33Z
dc.date.available 2019-12-20T18:17:33Z
dc.date.issued 2012
dc.identifier.uri http://sedici.unlp.edu.ar/handle/10915/87841
dc.description.abstract β2-syntrophin, a dystrophin-associated protein, plays a pivotal role in insulin secretion by pancreatic β-cells. It contains a PDZ domain (β2S-PDZ) that, in complex with protein-tyrosine phosphatase ICA512, anchors the dense insulin granules to actin filaments. The phosphorylation state of β2-syntrophin allosterically regulates the affinity of β2S-PDZ for ICA512, and the disruption of the complex triggers the mobilization of the insulin granule stores. Here, we investigate the thermal unfolding of β2S-PDZ at different pH and urea concentrations. Our results indicate that, unlike other PDZ domains, β2S-PDZ is marginally stable. Thermal denaturation experiments show broad transitions and cold denaturation, and a two-state model fit reveals a significant unfolded fraction under physiological conditions. Furthermore, Tm and Tmax denaturant-dependent shifts and noncoincidence of melting curves monitored at different wavelengths suggest that two-state and three-state models fail to explain the equilibrium data properly and are in better agreement with a downhill scenario. Its higher stability at pH > 9 and the results of molecular dynamics simulations indicate that this behavior of β2S-PDZ might be related to its charge distribution. All together, our results suggest a link between the conformational plasticity of the native ensemble of this PDZ domain and the regulation of insulin secretion. en
dc.format.extent 2835-2844 es
dc.language en es
dc.subject β2-syntrophin es
dc.subject PDZ domain es
dc.title Equilibrium unfolding of the PDZ domain of β2-syntrophin en
dc.type Articulo es
sedici.identifier.other doi:10.1016/j.bpj.2012.05.021 es
sedici.identifier.other eid:2-s2.0-84862639460 es
sedici.identifier.issn 0006-3495 es
sedici.creator.person Torchio, Gabriela María es
sedici.creator.person Ermácora, Mario Roberto es
sedici.creator.person Sica, Mauricio Pablo es
sedici.subject.materias Ciencias Exactas es
sedici.description.fulltext true es
mods.originInfo.place Instituto Multidisciplinario de Biología Celular es
sedici.subtype Articulo es
sedici.rights.license Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
sedici.rights.uri http://creativecommons.org/licenses/by-nc-sa/4.0/
sedici.description.peerReview peer-review es
sedici.relation.journalTitle Biophysical Journal es
sedici.relation.journalVolumeAndIssue vol. 102, no. 12 es
sedici.rights.sherpa * Color: amarillo* Pre-print del autor: si* Post-print del autor: restricted* Versión de editor/PDF:no* Condiciones:>>Author's pre-prints on private websites only>>Author's post-print on non-commercial hosting platforms including institutional repositories>>Debe ir enlazado a la versión de editor>>Deben reconocerse el copyright y la fuente editorial>>La versión de editor/PDF no puede utilizarse>>Publisher last contacted on 05/08/2015* Link a Sherpa: http://sherpa.ac.uk/romeo/issn/0006-3495/es/


Download Files

This item appears in the following Collection(s)

Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0) Except where otherwise noted, this item's license is described as Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)