Targeting of a tail anchored protein to Endoplasmic Reticulum and Mitochondrial Outer Membranes by independent and competing pathways (Articolo in rivista)

Type

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

Label

• Targeting of a tail anchored protein to Endoplasmic Reticulum and Mitochondrial Outer Membranes by independent and competing pathways (Articolo in rivista) (literal)

Anno

• 2001-01-01T00:00:00+01:00 (literal)

Alternative label

• Nica Borgese, Ilaria Gazzoni, Massimo Barberi, Sara Colombo, and Emanuela Pedrazzini (2001)
  Targeting of a tail anchored protein to Endoplasmic Reticulum and Mitochondrial Outer Membranes by independent and competing pathways
  in Molecular biology of the cell (Online)
  (literal)

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

• Nica Borgese, Ilaria Gazzoni, Massimo Barberi, Sara Colombo, and Emanuela Pedrazzini (literal)

Pagina inizio

• 2482 (literal)

Pagina fine

• 2496 (literal)

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

• http://www.molbiolcell.org/content/12/8/2482.full (literal)

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

• 12 (literal)

Rivista

• Molecular biology of the cell (Rivista)

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

• 8 (literal)

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

• NB, IG, MB, SC, EP: Consiglio Nazionale delle Ricerche, Cellular and Molecular Pharmacology Center and Department of Medical Pharmacology, University of Milan, Milan, Italy NB: Faculty of Pharmacy, University of Catanzaro \"Magna Graecia,\" Catanzaro, Italy (literal)

Titolo

• Targeting of a tail anchored protein to Endoplasmic Reticulum and Mitochondrial Outer Membranes by independent and competing pathways (literal)

Abstract

• Many mitochondrial outer membrane (MOM) proteins have a transmembrane domain near the C terminus and an N-terminal cytosolic moiety. It is not clear how these tail-anchored (TA) proteins posttranslationally select their target, but C-terminal charged residues play an important role. To investigate how discrimination between MOM and endoplasmic reticulum (ER) occurs, we used mammalian cytochrome b 5, a TA protein existing in two, MOM or ER localized, versions. Substitution of the seven C-terminal residues of the ER isoform or of green fluorescent protein reporter constructs with one or two arginines resulted in MOM-targeted proteins, whereas a single C-terminal threonine caused promiscuous localization. To investigate whether targeting to MOM occurs from the cytosol or after transit through the ER, we tagged a MOM-directed construct with a C-terminal N-glycosylation sequence. Although in vitro this construct was efficiently glycosylated by microsomes, the protein expressed in vivo localized almost exclusively to MOM, and was nearly completely unglycosylated. The small fraction of glycosylated protein was in the ER and was not a precursor to the unglycosylated form. Thus, targeting occurs directly from the cytosol. Moreover, ER and MOM compete for the same polypeptide, explaining the dual localization of some TA proteins. (literal)

Prodotto di

• Institute of agricultural biology and biotechnology (IBBA) (Istituto)
• Istituto di neuroscienze (IN) (Istituto)

Autore CNR

• EMANUELA PEDRAZZINI (Unità di personale interno)
• SARA FRANCESCA COLOMBO (Unità di personale interno)
• DOMINICA BORGESE (Unità di personale esterno)

Incoming links:

Prodotto

• Institute of agricultural biology and biotechnology (IBBA) (Istituto)
• Istituto di neuroscienze (IN) (Istituto)

Autore CNR di

• EMANUELA PEDRAZZINI (Unità di personale interno)
• DOMINICA BORGESE (Unità di personale esterno)
• SARA FRANCESCA COLOMBO (Unità di personale interno)

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

• Molecular biology of the cell (Rivista)