Recycling of proteins from the Golgi compartment to the ER in yeast.

Dean, Neta; Pelham, Hugh R.B.

doi:10.1083/jcb.111.2.369

Cited by 184 publications

(116 citation statements)

References 27 publications

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“…3A, triangle) by cis-Golgi-specific mannosidase activity. B-Glyc-KDEL thus cycles between ER and cis-Golgi compartments, as described for other resident ER proteins (1,5). The same results on glycosylation of B-Glyc-KDEL were obtained in A431 cells and Vero cells (not shown).…”

Section: Shiga Toxin B-fragment With An N-glycosylation Site and The supporting

confidence: 70%

Retrograde Transport of KDEL-bearing B-fragment of Shiga Toxin

Johannes¹,

Tenza

Antony

et al. 1997

Journal of Biological Chemistry

187

254

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To investigate retrograde transport along the biosynthetic/secretory pathway, we have constructed a recombinant Shiga toxin B-fragment carrying an N-glycosylation site and a KDEL retrieval motif at its carboxyl terminus (B-Glyc-KDEL). After incubation with HeLa cells, B-Glyc-KDEL was progressively glycosylated in the endoplasmic reticulum (ER) and remained stably associated with this compartment. B-fragment with a nonfunctional KDEL sequence (B-Glyc-KDELGL) was glycosylated with about the same kinetics as B-Glyc-KDEL but localized at steady state to the Golgi apparatus. Morphological studies showed that B-Glyc-KDEL was delivered from the plasma membrane, via endosomes and the cisternae of the Golgi apparatus, to the ER. Moreover, the addition of a sulfation site allowed us to show that B-Glyc-KDEL on transit to the ER entered the Golgi apparatus through the trans-Golgi network. Transport of B-Glyc-KDEL to the ER was slowed down by nocodazole, indicating that microtubules are important for the retrograde pathway. Our results document the existence of a continuous pathway from the plasma membrane to the endoplasmic reticulum via the Golgi apparatus and show that a fully folded exogenous protein arriving in the endoplasmic reticulum via this pathway can undergo N-glycosylation.

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Section: Shiga Toxin B-fragment With An N-glycosylation Site and The supporting

confidence: 70%

Retrograde Transport of KDEL-bearing B-fragment of Shiga Toxin

Johannes¹,

Tenza

Antony

et al. 1997

Journal of Biological Chemistry

187

254

View full text Add to dashboard Cite

show abstract

“…The mutant proteins might be retained in the ER or, alternatively, delivered to the Golgi and rapidly transported back into the ER (Dean and Pelham, 1990). The latter mechanism would lead to Golgi-specific limited outer-chain glycosyl modification of the core glycosylated mutant proteins.…”

Section: Pra* and Cpy* Are Not A-1+6 Or A-1-+3 Mannosylatedmentioning

confidence: 99%

Analysis of two mutated vacuolar proteins reveals a degradation pathway in the endoplasmic reticulum or a related compartment of yeast

Finger

Knop

Wolf

1993

European Journal of Biochemistry

194

174

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The fate of a mutant form of each of the two yeast vacuolar enzymes proteinase yscA (PrA) and carboxypeptidase yscY (CPY) has been investigated. Both mutant proteins are rapidly degraded after entering the secretory pathway. Mutant PrA is deleted in 37 amino acids spanning the processing site region of the PrA pro‐peptide. The mutant enzyme shows no activity towards maturation of itself or other vacuolar hydrolases, a function of wild‐type PrA. Mutant CPY carries an Arg instead of a Gly residue in a highly conserved region, two positions distant from the active‐site Ser. In contrast to wild‐type CPY, the mutant form was quickly degraded by trypsin in vitro, indicating an altered structure. Using antisera specific for α‐1→6 and α‐1→3 outer‐chain mannose linkages, no Golgi‐specific carbohydrate modification could be detected on either mutant protein. Subcellular fractionation studies located both mutant enzymes in the endoplasmic reticulum. Degradation kinetics of both proteins show the same characteristics, indicating similar degradation pathways. The degradation process was shown to be independent of a functional sec18 gene product and takes place before Golgi‐specific carbohydrate modifications occur. The proteasome, the major proteolytic activity of the cytoplasm, is not involved in this degradation event. All degradation characteristics of the two mutant proteins are consistent with a degradation process within the endoplasmic reticulum (‘ER degradation’).

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“…lnvertase and pro-a factor fusion constructs were identical to those used previously (Pelham et al, 1988;Dean and Pelham, 1990) except that additional constructs encoding proteins terminating with YFDDEL were prepared using synthetic oligonucleotides. All were inserted at the URA3 locus.…”

Section: Cloningmentioning

confidence: 99%

The ERD2 gene determines the specificity of the luminal ER protein retention system

Lewis

Sweet

Pelham

1990

Cell

227

114

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SummaryLuminal ER proteins carry a signal at their C terminus that prevents their secretion; in S. cerevisiae this signal is the tetrapeptide HDEL. Indirect evidence suggests that HDEL is recognized by a receptor that retrieves ER proteins from the secretory pathway and returns them to the ER, and a candidate for this receptor is the product of the ERDP gene (see accompanying paper). We show here that presumptive ER proteins from the budding yeast K. lactis can terminate either with HDEL or, in the case of BiP, with DDEL. S. cerevisiae does not efficiently recognize DDEL as a retention signal, but exchange of its ERD2 gene for the corresponding gene from K. lactis allows equal recognition of DDEL and HDEL. Thus the specificity of the retention system is determined by the ERD2 gene. We conclude that ERDP encodes the receptor that sorts luminal ER proteins.

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Recycling of proteins from the Golgi compartment to the ER in yeast.

Cited by 184 publications

References 27 publications

Retrograde Transport of KDEL-bearing B-fragment of Shiga Toxin

Retrograde Transport of KDEL-bearing B-fragment of Shiga Toxin

Analysis of two mutated vacuolar proteins reveals a degradation pathway in the endoplasmic reticulum or a related compartment of yeast

The ERD2 gene determines the specificity of the luminal ER protein retention system

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