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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/17991
Ver los metadatos del registro completo
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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 Técnicas2025-09-29T09:38:06Zoai: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:34982025-09-29 09:38:06.717CONICET 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_ |
1844613203712016384 |
score |
13.070432 |