Protein folding in the ER

Stevens, Fred J.; Argon, Yair

doi:10.1006/scdb.1999.0315

Cited by 155 publications

(113 citation statements)

References 102 publications

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“…Protein density in the ER is extremely high, around 100 mg/ml, together with concomitant protein manufacturing (Stevens and Argon 1999). Therefore, the elaborate proteostasis network described above is vital.…”

Section: Therapeutic Perspectivesmentioning

confidence: 99%

Protein Folding and Quality Control in the ER

Araki

Nagata

2011

Cold Spring Harbor Perspectives in Biology

317

285

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The endoplasmic reticulum (ER) uses an elaborate surveillance system called the ER quality control (ERQC) system. The ERQC facilitates folding and modification of secretory and membrane proteins and eliminates terminally misfolded polypeptides through ER-associated degradation (ERAD) or autophagic degradation. This mechanism of ER protein surveillance is closely linked to redox and calcium homeostasis in the ER, whose balance is presumed to be regulated by a specific cellular compartment. The potential to modulate proteostasis and metabolism with chemical compounds or targeted siRNAs may offer an ideal option for the treatment of disease.

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Section: Therapeutic Perspectivesmentioning

confidence: 99%

Protein Folding and Quality Control in the ER

Araki

Nagata

2011

Cold Spring Harbor Perspectives in Biology

317

285

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“…Mammalian cells contain three classes of PPIs: parvulins, cyclophilins (Cyps), and FK506-binding proteins (48). ADAMTS13, harboring 118 prolines, contains a higher number of proline residues and thus needs PPIases activity to fold and maturate correctly in the cell.…”

Section: Page 15 Of 30mentioning

confidence: 99%

The D173G mutation in ADAMTS-13 causes a severe form of congenital thrombotic thrombocytopenic purpura

Lancellotti¹,

Peyvandi²,

Pagliari³

et al. 2016

Thromb Haemost

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“…1 Glycosylation and disulfide bond formation are involved in the correct folding of these proteins because inhibition of such post-translational modifications causes accumulation of unfolded proteins in the ER. As described below, various molecular chaperones and folding enzymes located in the ER play crucial roles in these cellular events (1).…”

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confidence: 99%

“…ac.jp. 1 The abbreviations used are: ER, endoplasmic reticulum; PDI, protein disulfide isomerase; JPDI, J-domain-containing PDI-like protein; EST, expressed sequence tag; HA, hemagglutinin; JPDI-HA, HA-tagged JPDI; EndoH, endo-␤-N-acetylglucosaminidase H; GST, glutathione S-transferase; GST-J, a fusion of GST-JPDI J-domain (His) 6 tag; Trx-100, Triton X-100; CBB, Coomassie Brilliant Blue R-250; RACE, rapid amplification of cDNA ends. ER carry a conserved tetrapeptide sequence, KDEL, at their C terminus (25).…”

mentioning

confidence: 99%

JPDI, a Novel Endoplasmic Reticulum-resident Protein Containing Both a BiP-interacting J-domain and Thioredoxin-like Motifs

Hosoda

Kimata

Tsuru

et al. 2003

Journal of Biological Chemistry

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Several endoplasmic reticulum (ER)-resident luminalproteins have a characteristic ER retrieval signal, KDEL, or its variants at their C terminus. Our previous work searching EST databases for proteins containing the C-terminal KDEL motif predicted some novel murine proteins, one of which designated JPDI (J-domaincontaining protein disulfide isomerase-like protein) is characterized in this study. The primary structure of JPDI is unique, because in addition to a J-domain motif adjacent to the N-terminal translocation signal sequence, four thioredoxin-like motifs were found in a single polypeptide. As examined by Northern blotting, the expression of JPDI was essentially ubiquitous in tissues and almost independent of ER stress. A computational prediction that JPDI is an ER-resident luminal protein was experimentally supported by immunofluorescent staining of epitope-tagged JPDI-expressing cells together with glycosylation and protease protection studies of this protein. JPDI probably acts as a DnaJlike partner of BiP, because a recombinant protein carrying the J-domain of JPDI associated with BiP in an ATP-dependent manner and enhanced its ATPase activity. We speculate that for the folding of some proteins in the ER, chaperoning by BiP and formation of proper disulfide bonds may synchronously occur in a JPDI-dependent manner.

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Protein folding in the ER

Cited by 155 publications

References 102 publications

Protein Folding and Quality Control in the ER

Protein Folding and Quality Control in the ER

The D173G mutation in ADAMTS-13 causes a severe form of congenital thrombotic thrombocytopenic purpura

JPDI, a Novel Endoplasmic Reticulum-resident Protein Containing Both a BiP-interacting J-domain and Thioredoxin-like Motifs

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