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N-Linked Glycosylation of the p24 Family Protein p24δ5 Modulates Retrograde Golgi-to-ER Transport of K/HDEL Ligands in Arabidopsis

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N-Linked Glycosylation of the p24 Family Protein p24δ5 Modulates Retrograde Golgi-to-ER Transport of K/HDEL Ligands in Arabidopsis

dc.contributor.author	Pastor Cantizano, Noelia
dc.contributor.author	García Murria, María Jesús
dc.contributor.author	Bernat Silvestre, César
dc.contributor.author	Marcote Zaragoza, María Jesús
dc.contributor.author	Mingarro Muñoz, Ismael
dc.contributor.author	Aniento Company, Fernando
dc.date.accessioned	2019-11-12T11:35:01Z
dc.date.available	2019-11-12T11:35:01Z
dc.date.issued	2017
dc.identifier.citation	Pastor Cantizano, Noelia García Murria, María Jesús Bernat Silvestre, César Marcote Zaragoza, María Jesús Mingarro Muñoz, Ismael Aniento Company, Fernando 2017 N-Linked Glycosylation of the p24 Family Protein p24δ5 Modulates Retrograde Golgi-to-ER Transport of K/HDEL Ligands in Arabidopsis Molecular Plant 10 8 1095 1106
dc.identifier.uri	https://hdl.handle.net/10550/72176
dc.description.abstract	The K/HDEL receptor ERD2 mediates the transport of soluble endoplasmic reticulum (ER)-resident proteins containing a C-terminal K/HDEL signal from the Golgi apparatus back to the ER via COPI (COat Protein I)-coated vesicles. Sorting of ERD2 within COPI vesicles is facilitated by p24 proteins. In Arabidopsis, p24δ5 has been shown to interact directly with ERD2 via its luminal GOLD (GOLgi Dynamics) domain and with COPI proteins via its cytoplasmic C-terminal tail at the acidic pH of the Golgi apparatus. Several members of the p24 family in mammals and yeast have been shown to be glycosylated, but whether Arabidopsis p24 proteins are glycosylated and the role of the sugar moiety in p24 function remain unclear. Here, we show that Arabidopsis p24δ5 protein is N-glycosylated in its GOLD domain. Furthermore, we demonstrate that this post-translational modification is important for its coupled transport with p24β2 at the ER-Golgi interface, for its interaction with the K/HDEL receptor ERD2, and for retrograde transport of ERD2 and K/HDEL ligands from the Golgi apparatus back to the ER.
dc.language.iso	eng
dc.relation.ispartof	Molecular Plant, 2017, vol. 10, num. 8, p. 1095-1106
dc.subject	Biotecnologia
dc.subject	Proteïnes
dc.title	N-Linked Glycosylation of the p24 Family Protein p24δ5 Modulates Retrograde Golgi-to-ER Transport of K/HDEL Ligands in Arabidopsis
dc.type	journal article	es_ES
dc.date.updated	2019-11-12T11:35:01Z
dc.identifier.doi	10.1016/j.molp.2017.07.007
dc.identifier.idgrec	123477
dc.rights.accessRights	open access	es_ES