http://www.cnr.it/ontology/cnr/individuo/prodotto/ID258411

Misfolding and aggregation of vacuolar glycoproteins in plant cells (Articolo in rivista)

Type

Articolo in rivista (Classe)
Prodotto della ricerca (Classe)

Label

Misfolding and aggregation of vacuolar glycoproteins in plant cells (Articolo in rivista) (literal)

Anno

2000-01-01T00:00:00+01:00 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

10.1111/j.1365-313X.2000.00933.x (literal)

Alternative label

Sparvoli Francesca Faoro Franco Daminati Maria Gloria Ceriotti Aldo Bollini Roberto (2000)
Misfolding and aggregation of vacuolar glycoproteins in plant cells
in Plant journal (Online); Wiley-Blackwell, Oxford (Regno Unito)
(literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

Sparvoli Francesca Faoro Franco Daminati Maria Gloria Ceriotti Aldo Bollini Roberto (literal)

Pagina inizio

825 (literal)

Pagina fine

836 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url

http://onlinelibrary.wiley.com/doi/10.1111/j.1365-313X.2000.00933.x/abstract (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

24 (literal)

Rivista

Plant journal (Rivista)

Note

Scopus (literal)
PubMed (literal)
ISI Web of Science (WOS) (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

Sparvoli Francesca, Daminati Maria Gloria, Ceriotti Aldo, Bollini Roberto IBBA-CNR Faoro Franco IVV-CNR (literal)

Titolo

Misfolding and aggregation of vacuolar glycoproteins in plant cells (literal)

Abstract

Phaseolin and lectin-related polypeptides, the abundant oligomeric glycoproteins of bean seeds, are synthesized on the endoplasmic reticulum (ER) and then transported to the storage vacuole via the Golgi apparatus. Glycosylation and folding are among the major modifications these proteins undergo in the ER. Although a recurrent role of N-glycosylation is on protein folding, in previous studies on common bean (Phaseolus vulgaris) seeds we demonstrated that the oligosaccharide side-chains are not required for folding, intracellular transport and activity of storage glycoproteins. We show here that in lima bean (Phaseolus lunatus), incubation of the developing cotyledon with tunicamycin to prevent glycosylation has a dramatic effect on the intracellular transport of the storage glycoproteins. When lacking their glycans, phaseolin and lectin-related polypeptides misfold and are retained in the ER as mixed aggregates to which the chaperone BiP irreversibly associates. The lumen of the ER becomes enlarged to accommodate the aggregated polypeptides. Intracellular transport of legumin, a naturally unglycosylated storage protein, is mostly unaffected by the inhibitor, indicating that the observed phenomenon specifically occurs on glycoproteins. Furthermore, recombinant lima bean phaseolin synthesized in tobacco protoplasts is also correctly folded and matured in the presence of tunicamycin. To our knowledge, this is the first report that describes in detail the block of intracellular transport of vacuolar glycoproteins in plant cells due to aggregation following glycosylation inhibition. (literal)

Editore