title: Influence of KDEL on the fate of trimeric or assembly-defective phaseolin: selective use of an alternative route to vacuoles.
abstract: The tetrapeptide KDEL is commonly found at the C terminus of soluble proteins of the endoplasmic reticulum (ER), and it contributes to their localization by interacting with a receptor that recycles between the Golgi complex and the ER. We investigated the effects of the addition of KDEL to phaseolin, a protein normally delivered from the ER to storage vacuoles via the Golgi complex. We show that KDEL prevents acquisition of trans-Golgi-specific glycan modifications and causes interactions with the chaperone BiP that are distinct from the ones between BiP and defective proteins. KDEL markedly increases the stability of phaseolin, but a small proportion of phaseolin-KDEL slowly reaches the vacuole without undergoing Golgi-mediated glycan modifications, in a process that can be inhibited by brefeldin A but not monensin. Our results indicate that KDEL can operate with high efficiency before proteins can reach the late Golgi cisternae but allows or promotes delivery to vacuoles via an alternative mechanism. However, addition of KDEL does not alter the destiny of an assembly-defective form of phaseolin, suggesting that the plant ER quality control mechanism is dominant over KDEL effects.
authors.affiliation: Istituto Biosintesi Vegetali, Consiglio Nazionale delle Ricerche, 20133 Milano, Italy.
authors.forename: L
authors.initials: L
authors.lastname: Frigerio
authors.forename: A
authors.initials: A
authors.lastname: Pastres
authors.forename: A
authors.initials: A
authors.lastname: Prada
authors.forename: A
authors.initials: A
authors.lastname: Vitale
mesh_terms: D002352:Carrier Proteins / Q000378:metabolism; D002451:Cell Compartmentation; D004721:Endoplasmic Reticulum / Q000378:metabolism; D000091342:Endoplasmic Reticulum Chaperone BiP; D006056:Golgi Apparatus / Q000378:metabolism; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones / Q000378:metabolism; D009842:Oligopeptides / Q000378:metabolism*; D018515:Plant Leaves / Q000166:cytology / Q000378:metabolism; D010940:Plant Proteins / Q000378:metabolism*; D030821:Plants, Genetically Modified; D010947:Plants, Toxic; D011487:Protein Conformation; D021382:Protein Sorting Signals; D021381:Protein Transport; D011523:Protoplasts / Q000378:metabolism; D014026:Nicotiana; D014617:Vacuoles / Q000378:metabolism*
chemical_list: D002352:Carrier Proteins; D000091342:Endoplasmic Reticulum Chaperone BiP; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D009842:Oligopeptides; D010940:Plant Proteins; D021382:Protein Sorting Signals; C048826:phaseolin protein, Phaseolus vulgaris; C073762:lysyl-aspartyl-glutamyl-leucine