A CHIMERIC PROTEIN WITH HIGH AFFINITY TO THE ENDOPLASMIC RETICULUM CHAPERONE BIP IS DELIVERED TO THE VACUOLE IN PLANT CELLS. (Contributo in atti di convegno)

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Label
  • A CHIMERIC PROTEIN WITH HIGH AFFINITY TO THE ENDOPLASMIC RETICULUM CHAPERONE BIP IS DELIVERED TO THE VACUOLE IN PLANT CELLS. (Contributo in atti di convegno) (literal)
Anno
  • 2008-01-01T00:00:00+01:00 (literal)
Alternative label
  • Ombretta Foresti, Francesca De Marchis, Maddalena de Virgilio, Eva M. Klein, Sergio Arcioni, Michele Bellucci and Alessandro Vitale (2008)
    A CHIMERIC PROTEIN WITH HIGH AFFINITY TO THE ENDOPLASMIC RETICULUM CHAPERONE BIP IS DELIVERED TO THE VACUOLE IN PLANT CELLS.
    in XI ENPER Informal Meeting, Lecce
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Ombretta Foresti, Francesca De Marchis, Maddalena de Virgilio, Eva M. Klein, Sergio Arcioni, Michele Bellucci and Alessandro Vitale (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#descrizioneSinteticaDelProdotto
  • The correct folding and assembly of newly synthesized secretory proteins are monitored by the protein quality control system of the endoplasmic reticulum (ER). Through interactions with chaperones such as the binding protein (BiP) and other folding helpers, quality control favours productive folding and sorts for degradation aberrant proteins. A major route for quality control degradation identified in yeast, plants and animals is constituted by retrotranslocation from the ER to the cytosol and subsequent disposal by the ubiquitin/proteasome system, but alternative routes involving the vacuole have been identified in yeast. In this study, we have followed the fate of sGFP418, a fusion between a secretory form of GFP and a domain of the vacuolar protein phaseolin that is involved in correct trimer formation and in BiP recognition of unassembled subunits. We show that sGFP418 is delivered to the vacuole and fragmented, in a process that, similarly to normal phaseolin sorting to the vacuole, can be fully blocked by the protein traffic inhibitor brefeldin A. A fusion between GFP and a domain of the maize storage protein ã-zein involved in zein polymerization also undergoes post-translational fragmentation similar to that of sGFP418. Because sGFP418 does not contain the vacuolar sorting signal of phaseolin and the zein domain promotes assembly into protein bodies within the ER when fused to other protein sequences, these results strongly suggest the existence of a plant vacuolar sorting mechanism devoted to the disposal of defective secretory proteins that are not retrotranslocated but expose sequences normally involved in oligomerization. (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Istituto di Biologia e Biotecnologia Agraria, Consiglio Nazionale delle Ricerche, via Bassini 15, 20133 Milano Italy, European Union Istituto Genetica Vegetale, Consiglio Nazionale delle Ricerche, Articolazione Territoriale di Perugia, via della Madonna Alta 130, 06128 Perugia, Italy, European Union Present address: Istituto Genetica Vegetale, Consiglio Nazionale delle Ricerche, Via G. Amendola 165/A, 70126 Bari, Italy, European Union (literal)
Titolo
  • A CHIMERIC PROTEIN WITH HIGH AFFINITY TO THE ENDOPLASMIC RETICULUM CHAPERONE BIP IS DELIVERED TO THE VACUOLE IN PLANT CELLS. (literal)
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