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dc.contributor.author
Vartak, Nachiket
dc.contributor.author
Papke, Bjoern
dc.contributor.author
Grecco, Hernan Edgardo
dc.contributor.author
Rossmannek, Lisaweta
dc.contributor.author
Waldmann, Herbert
dc.contributor.author
Hedberg, Christian
dc.contributor.author
Bastiaens, Philippe I. H.
dc.date.available
2017-06-12T15:53:50Z
dc.date.issued
2014-01
dc.identifier.citation
Vartak, 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.identifier.issn
0006-3495
dc.identifier.uri
http://hdl.handle.net/11336/17991
dc.description.abstract
The 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.format
application/pdf
dc.language.iso
eng
dc.publisher
Cell Press
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Palmitoylation
dc.subject
Fret
dc.subject
Apt
dc.subject.classification
Biología Celular, Microbiología
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Ciencias Biológicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
The Autodepalmitoylating activity of APT maintains the spatial organization of Palmitoylated membrane proteins
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2017-06-09T14:15:41Z
dc.journal.volume
106
dc.journal.number
1
dc.journal.pagination
93-105
dc.journal.pais
Estados Unidos
dc.journal.ciudad
Massachusetts
dc.description.fil
Fil: Vartak, Nachiket. Institut Max Planck Fur Molekulare Physiologie; Alemania
dc.description.fil
Fil: Papke, Bjoern. Institut Max Planck Fur Molekulare Physiologie; Alemania
dc.description.fil
Fil: Grecco, Hernan Edgardo. Institut Max Planck Fur Molekulare Physiologie; Alemania. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.description.fil
Fil: Rossmannek, Lisaweta. Institut Max Planck Fur Molekulare Physiologie; Alemania
dc.description.fil
Fil: Waldmann, Herbert. Institut Max Planck Fur Molekulare Physiologie; Alemania
dc.description.fil
Fil: Hedberg, Christian. Institut Max Planck Fur Molekulare Physiologie; Alemania
dc.description.fil
Fil: Bastiaens, Philippe I. H.. Institut Max Planck Fur Molekulare Physiologie; Alemania
dc.journal.title
Biophysical Journal
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1016/j.bpj.2013.11.024
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0006349513012587?via%3Dihub
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