The Autodepalmitoylating activity of APT maintains the spatial organization of Palmitoylated membrane proteins

Autores
Vartak, Nachiket; Papke, Bjoern; Grecco, Hernan Edgardo; Rossmannek, Lisaweta; Waldmann, Herbert; Hedberg, Christian; Bastiaens, Philippe I. H.
Año de publicación
2014
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
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.
Fil: Vartak, Nachiket. Institut Max Planck Fur Molekulare Physiologie; Alemania
Fil: Papke, Bjoern. Institut Max Planck Fur Molekulare Physiologie; Alemania
Fil: Grecco, Hernan Edgardo. Institut Max Planck Fur Molekulare Physiologie; Alemania. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Rossmannek, Lisaweta. Institut Max Planck Fur Molekulare Physiologie; Alemania
Fil: Waldmann, Herbert. Institut Max Planck Fur Molekulare Physiologie; Alemania
Fil: Hedberg, Christian. Institut Max Planck Fur Molekulare Physiologie; Alemania
Fil: Bastiaens, Philippe I. H.. Institut Max Planck Fur Molekulare Physiologie; Alemania
Materia
Palmitoylation
FRET
APT
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/17991
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/17991
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling The Autodepalmitoylating activity of APT maintains the spatial organization of Palmitoylated membrane proteinsVartak, NachiketPapke, BjoernGrecco, Hernan EdgardoRossmannek, LisawetaWaldmann, HerbertHedberg, ChristianBastiaens, Philippe I. H.PalmitoylationFRETAPThttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The 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.Fil: Vartak, Nachiket. Institut Max Planck Fur Molekulare Physiologie; AlemaniaFil: Papke, Bjoern. Institut Max Planck Fur Molekulare Physiologie; AlemaniaFil: Grecco, Hernan Edgardo. Institut Max Planck Fur Molekulare Physiologie; Alemania. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Rossmannek, Lisaweta. Institut Max Planck Fur Molekulare Physiologie; AlemaniaFil: Waldmann, Herbert. Institut Max Planck Fur Molekulare Physiologie; AlemaniaFil: Hedberg, Christian. Institut Max Planck Fur Molekulare Physiologie; AlemaniaFil: Bastiaens, Philippe I. H.. Institut Max Planck Fur Molekulare Physiologie; AlemaniaCell Press2014-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/17991Vartak, 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; 93-1050006-3495enginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.bpj.2013.11.024info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0006349513012587?via%3Dihubinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T11:06:21Zoai:ri.conicet.gov.ar:11336/17991instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-10-22 11:06:21.24CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv The Autodepalmitoylating activity of APT maintains the spatial organization of Palmitoylated membrane proteins
title The Autodepalmitoylating activity of APT maintains the spatial organization of Palmitoylated membrane proteins
spellingShingle The Autodepalmitoylating activity of APT maintains the spatial organization of Palmitoylated membrane proteins
Vartak, Nachiket
Palmitoylation
FRET
APT
title_short The Autodepalmitoylating activity of APT maintains the spatial organization of Palmitoylated membrane proteins
title_full The Autodepalmitoylating activity of APT maintains the spatial organization of Palmitoylated membrane proteins
title_fullStr The Autodepalmitoylating activity of APT maintains the spatial organization of Palmitoylated membrane proteins
title_full_unstemmed The Autodepalmitoylating activity of APT maintains the spatial organization of Palmitoylated membrane proteins
title_sort The Autodepalmitoylating activity of APT maintains the spatial organization of Palmitoylated membrane proteins
dc.creator.none.fl_str_mv Vartak, Nachiket
Papke, Bjoern
Grecco, Hernan Edgardo
Rossmannek, Lisaweta
Waldmann, Herbert
Hedberg, Christian
Bastiaens, Philippe I. H.
author Vartak, Nachiket
author_facet Vartak, Nachiket
Papke, Bjoern
Grecco, Hernan Edgardo
Rossmannek, Lisaweta
Waldmann, Herbert
Hedberg, Christian
Bastiaens, Philippe I. H.
author_role author
author2 Papke, Bjoern
Grecco, Hernan Edgardo
Rossmannek, Lisaweta
Waldmann, Herbert
Hedberg, Christian
Bastiaens, Philippe I. H.
author2_role author
author
author
author
author
author
dc.subject.none.fl_str_mv Palmitoylation
FRET
APT
topic Palmitoylation
FRET
APT
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv 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.
Fil: Vartak, Nachiket. Institut Max Planck Fur Molekulare Physiologie; Alemania
Fil: Papke, Bjoern. Institut Max Planck Fur Molekulare Physiologie; Alemania
Fil: Grecco, Hernan Edgardo. Institut Max Planck Fur Molekulare Physiologie; Alemania. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Rossmannek, Lisaweta. Institut Max Planck Fur Molekulare Physiologie; Alemania
Fil: Waldmann, Herbert. Institut Max Planck Fur Molekulare Physiologie; Alemania
Fil: Hedberg, Christian. Institut Max Planck Fur Molekulare Physiologie; Alemania
Fil: Bastiaens, Philippe I. H.. Institut Max Planck Fur Molekulare Physiologie; Alemania
description 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.
publishDate 2014
dc.date.none.fl_str_mv 2014-01
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/17991
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
0006-3495
url http://hdl.handle.net/11336/17991
identifier_str_mv 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
0006-3495
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bpj.2013.11.024
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0006349513012587?via%3Dihub
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv Cell Press
publisher.none.fl_str_mv Cell Press
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
_version_ 1846781359763226624
score 12.982451

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