dc.creator | Cabrera Sánchez, Margarita | es |
dc.creator | Muñiz Guinea, Manuel | es |
dc.creator | Hidalgo Jiménez, Josefina | es |
dc.creator | Vega, Lucía | es |
dc.creator | Martín Rubio, María Esther | es |
dc.creator | Velasco López, Ángel | |
dc.date.accessioned | 2016-04-18T12:37:30Z | |
dc.date.available | 2016-04-18T12:37:30Z | |
dc.date.issued | 2003 | |
dc.identifier.citation | Cabrera Sánchez, M., Muñiz Guinea, M., Hidalgo Jiménez, J., Vega, L., Martín Rubio, M.E. y Velasco López, Á. (2003). The retrieval function of the KDEL receptor requires PKA phosphorylation of its C-terminus. Molecular Biology of the Cell, 14 (10), 4114-4125. | |
dc.identifier.issn | 1059-1524 | es |
dc.identifier.uri | http://hdl.handle.net/11441/40032 | |
dc.description.abstract | The KDEL receptor is a Golgi/intermediate compartment-located integral membrane protein that carries out the retrieval
of escaped ER proteins bearing a C-terminal KDEL sequence. This occurs throughout retrograde traffic mediated by
COPI-coated transport carriers. The role of the C-terminal cytoplasmic domain of the KDEL receptor in this process has
been investigated. Deletion of this domain did not affect receptor subcellular localization although cells expressing this
truncated form of the receptor failed to retain KDEL ligands intracellularly. Permeabilized cells incubated with ATP and
GTP exhibited tubular processes-mediated redistribution from the Golgi area to the ER of the wild-type receptor, whereas
the truncated form lacking the C-terminal domain remained concentrated in the Golgi. As revealed with a peptidebinding
assay, this domain did not interact with both coatomer and ARF-GAP unless serine 209 was mutated to aspartic
acid. In contrast, alanine replacement of serine 209 inhibited coatomer/ARF-GAP recruitment, receptor redistribution into
the ER, and intracellular retention of KDEL ligands. Serine 209 was phosphorylated by both cytosolic and recombinant
protein kinase A (PKA) catalytic subunit. Inhibition of endogenous PKA activity with H89 blocked Golgi-ER transport of
the native receptor but did not affect redistribution to the ER of a mutated form bearing aspartic acid at position 209. We
conclude that PKA phosphorylation of serine 209 is required for the retrograde transport of the KDEL receptor from the
Golgi complex to the ER from which the retrieval of proteins bearing the KDEL signal depends. | es |
dc.format | application/pdf | es |
dc.language.iso | eng | es |
dc.publisher | American Society for Cell Biology | es |
dc.relation.ispartof | Molecular Biology of the Cell, 14 (10), 4114-4125. | |
dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 Internacional | * |
dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 Internacional | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | * |
dc.title | The retrieval function of the KDEL receptor requires PKA phosphorylation of its C-terminus | es |
dc.type | info:eu-repo/semantics/article | es |
dcterms.identifier | https://ror.org/03yxnpp24 | |
dc.type.version | info:eu-repo/semantics/publishedVersion | es |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | es |
dc.contributor.affiliation | Universidad de Sevilla. Departamento de Biología Celular | es |
dc.relation.publisherversion | http://www.molbiolcell.org/content/14/10/4 | es |
dc.relation.publisherversion | http://dx.doi.org/10.1091/mbc.E03-04-0194 | |
dc.identifier.doi | 10.1091/mbc.E03-04-0194 | |
dc.journaltitle | Molecular Biology of the Cell | |
dc.publication.volumen | 14 | |
dc.publication.issue | 10 | |
dc.publication.initialPage | 4114 | |
dc.publication.endPage | 4125 | |
dc.identifier.idus | https://idus.us.es/xmlui/handle/11441/40032 | |