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dc.contributor.author
Solis, Gonzalo P.
dc.contributor.author
Kazemzadeh, Arghavan
dc.contributor.author
Abrami, Laurence
dc.contributor.author
Valnohova, Jana
dc.contributor.author
Alvarez, Cecilia Ines
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dc.contributor.author
van der Goot, F. Gisou
dc.contributor.author
Katanaev, Vladimir L.
dc.date.available
2023-08-02T17:11:20Z
dc.date.issued
2022-12
dc.identifier.citation
Solis, Gonzalo P.; Kazemzadeh, Arghavan; Abrami, Laurence; Valnohova, Jana; Alvarez, Cecilia Ines; et al.; Local and substrate-specific S-palmitoylation determines subcellular localization of Gαo; Nature Research; Nature Communications; 13; 1; 12-2022; 1-21
dc.identifier.uri
http://hdl.handle.net/11336/206600
dc.description.abstract
Peripheral membrane proteins (PMPs) associate with cellular membranes through post-translational modifications like S-palmitoylation. The Golgi apparatus is generally viewed as the transitory station where palmitoyl acyltransferases (PATs) modify PMPs, which are then transported to their ultimate destinations such as the plasma membrane (PM). However, little substrate specificity among the many PATs has been determined. Here we describe the inherent partitioning of Gαo – α-subunit of heterotrimeric Go proteins – to PM and Golgi, independent from Golgi-to-PM transport. A minimal code within Gαo N-terminus governs its compartmentalization and re-coding produces G protein versions with shifted localization. We establish the S-palmitoylation at the outer nuclear membrane assay (“SwissKASH”) to probe substrate specificity of PATs in intact cells. With this assay, we show that PATs localizing to different membrane compartments display remarkable substrate selectivity, which is the basis for PMP compartmentalization. Our findings uncover a mechanism governing protein localization and establish the basis for innovative drug discovery.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
Nature Research
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
S-palmitoylation
dc.subject
Gαo
dc.subject.classification
Bioquímica y Biología Molecular
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dc.subject.classification
Ciencias Biológicas
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dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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dc.title
Local and substrate-specific S-palmitoylation determines subcellular localization of Gαo
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2023-07-07T21:38:51Z
dc.identifier.eissn
2041-1723
dc.journal.volume
13
dc.journal.number
1
dc.journal.pagination
1-21
dc.journal.pais
Reino Unido
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dc.description.fil
Fil: Solis, Gonzalo P.. Universidad de Ginebra; Suiza
dc.description.fil
Fil: Kazemzadeh, Arghavan. Universidad de Ginebra; Suiza
dc.description.fil
Fil: Abrami, Laurence. Ecole Polytechnique Fédérale de Lausanne; Suiza
dc.description.fil
Fil: Valnohova, Jana. Universidad de Ginebra; Suiza
dc.description.fil
Fil: Alvarez, Cecilia Ines. Universidad Nacional de Córdoba; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Córdoba. Centro de Investigaciones en Bioquímica Clínica e Inmunología; Argentina
dc.description.fil
Fil: van der Goot, F. Gisou. Ecole Polytechnique Fédérale de Lausanne; Suiza
dc.description.fil
Fil: Katanaev, Vladimir L.. Far Eastern Federal University. Institute of Life Sciences and Biomedicine; Rusia. Universidad de Ginebra; Suiza
dc.journal.title
Nature Communications
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1038/s41467-022-29685-8
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.nature.com/articles/s41467-022-29685-8
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