ERp61 Is GRP58, a Stress-Inducible Luminal Endoplasmic Reticulum Protein, but Is Devoid of Phosphatidylinositide-Specific Phospholipase C Activity

Mazzarella, Richard; Marcus, N; Haugejorden, S. M.; Balcarek, J M; Baldassare, Joseph J.; Roy, Biswajit; Li, Lijing; Lee, Amy; Green, M.

doi:10.1006/abbi.1994.1064

Cited by 64 publications

(53 citation statements)

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“…Over the years, ERp57 has emerged in the literature under various names, including ERp61 [32,33], HIP-70 [34], Q-2 [35], ER-60 [36], ERp60 [12,37] and P58 [38].…”

Section: Discussionmentioning

confidence: 99%

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The transient association of ERp57 with N‐glycosylated proteins is regulated by glucose trimming

Wal

Oliver

High

1998

European Journal of Biochemistry

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The thiol-dependent reductase ERp57 has been shown to interact specifically with in vitro synthesised glycoproteins imported into canine pancreatic microsomes. On this basis, it was proposed that ERp57 forms part of a glycoprotein-specific folding 'machinery', present in the lumen of the endoplasmic reticulum (ER). In this study, we have investigated the interaction of ERp57 with newly synthesised proteins using semi-permeabilised mammalian cells (SP cells), in which the ER remains essentially intact and, hence, resembles that of a living cell. We demonstrate that ERp57 interacts preferentially with the glycosylated versions of soluble and membrane proteins, and that this interaction occurs in combination with calnexin and calreticulin. For the first time, we have performed a detailed analysis of the kinetics of ERp57 binding to newly synthesised glycoproteins. We find that ERp57 associates transiently with glycoproteins Ϫ a characteristic of molecular chaperones. Using mutant SP cells deficient in glucosidase I, we confirm that the binding of ERp57 to glycoproteins depends upon glucose trimming. We also demonstrate, for the first time, that the release of ERp57 from glycoprotein substrates is dependent upon glucose trimming. These data are combined to present a unified model for the role of ERp57/ER lectin complexes during glycoprotein folding in vivo.Keywords : endoplasmic reticulum ; ERp57/GRP58 ; molecular chaperone ; N-linked glycosylation; protein disulphide isomerase.The endoplasmic reticulum (ER) membrane is a primary site of protein synthesis in mammalian cells. Newly synthesised proteins are inserted into, or translocated across, the ER membrane, from where they can reach their final destination in one of the organelles of the secretory pathway, the plasma membrane or the cell exterior.To facilitate protein maturation, the ER is equipped with a number of membrane and soluble proteins involved in the processing, modification, folding and oligomeric assembly of newly synthesised polypeptides. ER proteins involved in protein maturation include folding enzymes, such as peptidylprolyl cisϪtrans isomerase and members of the protein disulphide isomerase (PDI) family, as well as molecular chaperones of the Hsp70 and Hsp90 class heat-shock proteins, such as immunoglobulin heavy-chain-binding protein (BiP/GRP78) and GRP94 [1].In addition to these folding enzymes and chaperones, the ER contains two proteins with lectin-like properties, namely the type-I membrane protein calnexin, and its soluble homologue, calreticulin. Calnexin and calreticulin associate transiently with a wide variety of N-glycosylated proteins, and were proposed to influence folding, oligomerisation and ER retention. Together with several enzymes that modify N-linked oligosaccharides, calnexin and calreticulin constitute an ER quality-control machinery for glycoproteins [2].Calnexin and calreticulin display a specificity for monoglucosylated oligosaccharides [2Ϫ4] that are generated in the ER by the combined actions of two A-glucosidases and a...

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“…Over the years, ERp57 has emerged in the literature under various names, including ERp61 [32,33], HIP-70 [34], Q-2 [35], ER-60 [36], ERp60 [12,37] and P58 [38].…”

Section: Discussionmentioning

confidence: 99%

“…ERp57 was first thought to be a phospholipase [39], but actual phospholipase activity was never detected [11,33,40]. 5.…”

Section: Discussionmentioning

confidence: 99%

The transient association of ERp57 with N‐glycosylated proteins is regulated by glucose trimming

Wal

Oliver

High

1998

European Journal of Biochemistry

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“…The protein has the retrieval sequence QEDL [145,146]. On the amino acid level, overall identity with PDI is 33 %, and identity with the a-b-bh-ah domains of ERp72 is 40 %.…”

Section: Erp57mentioning

confidence: 99%

“…On the amino acid level, overall identity with PDI is 33 %, and identity with the a-b-bh-ah domains of ERp72 is 40 %. The protein responds to stress stimuli in a manner similar to that of the glucose-regulated proteins GRp78 and GRp94 [146,147], and may be up-regulated additionally by oestrogens in brain tissue and by luteinizing-hormone-releasing hormone in the pituitary [148].…”

Section: Erp57mentioning

confidence: 99%

The protein disulphide-isomerase family: unravelling a string of folds

Ferrari

Söling

1999

Biochemical Journal

403

359

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The mammalian protein disulphide-isomerase (PDI) family encompasses several highly divergent proteins that are involved in the processing and maturation of secretory proteins in the endoplasmic reticulum. These proteins are characterized by the presence of one or more domains of roughly 95-110 amino acids related to the cytoplasmic protein thioredoxin. All but the PDI-D subfamily are composed entirely of repeats of such domains, with at least one domain containing and one domain lacking a redox-active -Cys-Xaa-Xaa-Cys-tetrapeptide. In addition to their known roles as redox catalysts and isomerases, the last few years have revealed additional functions of the PDI proteins,

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“…ER-60 (ERp61, HIP70, Q2, GRP58, or ERp57), [1][2][3][4][5] of which the amino acid sequence is similar to that of protein disulˆde isomerase (PDI), has been shown to be a multifunctional protein with proteolytic activity 1,[6][7][8] and disulˆde bond-dependent folding activity on polypeptides. [9][10][11][12][13] In addition, ER-60 homologues of nematodes ( Diroˆlaria immitis and Caenorhabditis elegans), and bovine and giardial PDIs have been shown to have transglutaminase (TGase; EC 2.3.2.13) activity.…”

mentioning

confidence: 99%