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dc.provenanceCONICET-
dc.creatorVartak, Nachiket-
dc.creatorPapke, Bjoern-
dc.creatorGrecco, Hernan Edgardo-
dc.creatorRossmannek, Lisaweta-
dc.creatorWaldmann, Herbert-
dc.creatorHedberg, Christian-
dc.creatorBastiaens, Philippe I. H.-
dc.date2017-06-12T15:53:50Z-
dc.date2017-06-12T15:53:50Z-
dc.date2014-01-
dc.date2017-06-09T14:15:41Z-
dc.date.accessioned2019-04-29T15:47:39Z-
dc.date.available2019-04-29T15:47:39Z-
dc.date.issued2014-01-
dc.identifierVartak, Nachiket; Papke, Bjoern; Grecco, Hernan Edgardo; Rossmannek, Lisaweta; Waldmann, Herbert; et al.; The Autodepalmitoylating activity of APT maintains the spatial organization of Palmitoylated membrane proteins; Cell Press; Biophysical Journal; 106; 1; 1-2014; 93-105-
dc.identifier0006-3495-
dc.identifierhttp://hdl.handle.net/11336/17991-
dc.identifier.urihttp://rodna.bn.gov.ar:8080/jspui/handle/bnmm/302181-
dc.descriptionThe localization and signaling of S-palmitoylated peripheral membrane proteins is sustained by an acylation cycle in which acyl protein thioesterases (APTs) depalmitoylate mislocalized palmitoylated proteins on endomembranes. However, the APTs are themselves reversibly S-palmitoylated, which localizes thioesterase activity to the site of the antagonistc palmitoylation activity on the Golgi. Here, we resolve this conundrum by showing that palmitoylation of APTs is labile due to autodepalmitoylation, creating two interconverting thioesterase pools: palmitoylated APT on the Golgi and depalmitoylated APT in the cytoplasm, with distinct functionality. By imaging APT-substrate catalytic intermediates, we show that it is the depalmitoylated soluble APT pool that depalmitoylates substrates on all membranes in the cell, thereby establishing its function as release factor of mislocalized palmitoylated proteins in the acylation cycle. The autodepalmitoylating activity on the Golgi constitutes a homeostatic regulation mechanism of APT levels at the Golgi that ensures robust partitioning of APT substrates between the plasma membrane and the Golgi.-
dc.descriptionFil: Vartak, Nachiket. Institut Max Planck Fur Molekulare Physiologie; Alemania-
dc.descriptionFil: Papke, Bjoern. Institut Max Planck Fur Molekulare Physiologie; Alemania-
dc.descriptionFil: Grecco, Hernan Edgardo. Institut Max Planck Fur Molekulare Physiologie; Alemania. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina-
dc.descriptionFil: Rossmannek, Lisaweta. Institut Max Planck Fur Molekulare Physiologie; Alemania-
dc.descriptionFil: Waldmann, Herbert. Institut Max Planck Fur Molekulare Physiologie; Alemania-
dc.descriptionFil: Hedberg, Christian. Institut Max Planck Fur Molekulare Physiologie; Alemania-
dc.descriptionFil: Bastiaens, Philippe I. H.. Institut Max Planck Fur Molekulare Physiologie; Alemania-
dc.formatapplication/pdf-
dc.formatapplication/pdf-
dc.languageeng-
dc.publisherCell Press-
dc.relationinfo:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.bpj.2013.11.024-
dc.relationinfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0006349513012587?via%3Dihub-
dc.rightsinfo:eu-repo/semantics/openAccess-
dc.rightshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/-
dc.sourcereponame:CONICET Digital (CONICET)-
dc.sourceinstname:Consejo Nacional de Investigaciones Científicas y Técnicas-
dc.sourceinstacron:CONICET-
dc.source.urihttp://hdl.handle.net/11336/17991-
dc.subjectPalmitoylation-
dc.subjectFRET-
dc.subjectAPT-
dc.subjectBiología Celular, Microbiología-
dc.subjectCiencias Biológicas-
dc.subjectCIENCIAS NATURALES Y EXACTAS-
dc.titleThe Autodepalmitoylating activity of APT maintains the spatial organization of Palmitoylated membrane proteins-
dc.typeinfo:eu-repo/semantics/article-
dc.typeinfo:eu-repo/semantics/publishedVersion-
dc.typeinfo:ar-repo/semantics/articulo-
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