[38] Protein disulfide-isomerase

Freedman, Robert B.; Hawkins, Hilary C.; McLaughlin, Stephen H.

doi:10.1016/0076-6879(95)51143-1

Cited by 40 publications

(25 citation statements)

References 20 publications

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“…Hence the disulphide form of the protein is much less stable than the corresponding disulphide of thioredoxin. This is reflected in the oxidative function of PDI, in contrast with the reductive role of thioredoxin [51,52].…”

Section: Pdi Modelmentioning

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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Section: Pdi Modelmentioning

confidence: 99%

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

Ferrari

Söling

1999

Biochemical Journal

403

359

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“…PDI is an oxidoreductase that was identified first as a highly abundant, essential protein in the lumen of the endoplasmic reticulum (ER), where it catalyzes the formation, reduction, and isomerization of disulfide bridges of nascent proteins during their folding in the ER (8,9). However, there is accumulating evidence that, similarly to RB60, additional PDI-like proteins might also carry out other biological functions and that they may reside in additional subcellular compartments.…”

mentioning

confidence: 99%

Dual targeting of the protein disulfide isomerase RB60 to the chloroplast and the endoplasmic reticulum

Levitan

Trebitsh

Kiss

et al. 2005

Proc. Natl. Acad. Sci. U.S.A.

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RB60 is an atypical protein disulfide isomerase (PDI) that functions as a member of a redox regulatory protein complex controlling translation in the chloroplast of Chlamydomonas reinhardtii, but also contains a C-terminal endoplasmic reticulum (ER) retention signal, -KDEL. Here, we show by fluorescence microscopy that RB60 resides in the chloroplast but also outside of the chloroplast colocalized with BiP, an ER marker protein. RB60 accumulates in microsomes that exhibit a typical ER magnesium-shift, and cotranslationally translocates into ER microsomes. The first 50-aa leader of RB60 is sufficient for both chloroplast and ER targeting. The leader is cleaved upon translocation into the ER, whereas it remains intact after import to the chloroplast. The leader sequence also contains an acidic domain that appears necessary for the protein's association with the thylakoid membranes. Based on these and additional results, we propose that the dual localization of RB60 occurs via the two conserved transport mechanisms, to the chloroplast and to the ER, that the chloroplast RB60 most likely carries an additional function in the ER, and that its mode of transport, including the differential cleavage of its N terminus, plays an important role in its suborganellar localization and organellarspecific function.dual subcellular localization ͉ redox-responsive regulator ͉ membrane association ͉ GFP

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“…At least in the case of BiP, the role of ATP in its chaperone function appears to be similar to the role of ATP in the function of Hsp7O in that both chaperones possess an ATPase activity and utilize ATP for dissociation from their polypeptide substrates (23). Other likely ER chaperones include members of the thioredoxin superfamily that are thought to participate in disulfide isomerization (protein disulfide isomerase, ERp72, and ERp5O) (20,24,25,33); proteins related to peptidyl-prolyl isomerases (FK506-binding protein 13 and ER cyclophilins) (26-28); and calcium-binding proteins calreticulin and calnexin (20,29,30).In recent years, many studies on the molecular mechanisms of cellular injury due to ischemia have focused largely on the functions of cytosolic stress proteins, leaving the involvement of molecular chaperones localized to other cellular compartments, including the ER, much less explored. However, many of the epithelial proteins whose function is believed to be disrupted by ischemia are secretory proteins initially folded and assembled in the ER.…”

mentioning

confidence: 99%

Perturbations in maturation of secretory proteins and their association with endoplasmic reticulum chaperones in a cell culture model for epithelial ischemia.

Kuznetsov

Bush

Zhang

et al. 1996

Proc. Natl. Acad. Sci. U.S.A.

121

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The effects of ischemia on the maturation of secretory proteins are not well understood. Among several events that occur during ischemia-reperfusion are a rapid and extensive decrease in ATP levels and an alteration of cellular oxidative state. Since the normal folding and assembly of secretory proteins are mediated by endoplasmic reticulum (ER) molecular chaperones, the function of which depends on ATP and maintenance of an appropriate redox environment, ischemia might be expected to perturb folding of secretory proteins. In this study, whole animal and cultured cell models for the epithelial ischemic state were used to examine this possibility. After Ischemia is a major cause of epithelial and other tissue injury and leads to a variety of cellular lesions. These include disruption of tight junctions, the subcortical actin cytoskeleton, cell-substratum interactions mediated by integrins, and possibly of other cellular structures and processes involved in the generation and maintenance of apical-basolateral protein polarity (1-3). On a biochemical level, ischemia and subsequent reperfusion are manifested by a variety of changes that include a rapid and severe decline in cellular ATP levels (4-7), alterations of cellular redox state, and perturbations of Na+/K+ ratio, intracellular pH, and intracellular Ca2+ homeostasis (7-9). Ischemia also leads to a cytosolic stress response manifested by impressive induction of the heat shock proteins (Hsps), especially the members of the Hsp7O family (6, 10, 11). Preinduction of Hsp70 appears to protect from future ischemic insult (12-15).Hsp7O, like a number of other proteins believed to function as molecular chaperones, participates in the ATP-dependent folding and assembly of a variety of newly synthesized cytosolic proteins (16). Proteins belonging to the Hsp7O family are also involved in the detection of misfolded or misassembled proteins and may play a role in targeting them for degradation (17). In ischemia, it is believed that the resulting ATP depletion leads to misfolding and aggregation of proteins (e.g., the actin cytoskeleton) and that Hsp7O participates in the refolding of these proteins and/or their degradation (18).Secretory (membrane and secreted) proteins are translocated into the lumen of the endoplasmic reticulum (ER) shortly after initiation of their synthesis. The ER lumen serves as a site for folding, assembly and degradation of secretory proteins. As in the case of Hsp7O-catalyzed folding of cytosolic proteins, the maturation of secretory proteins in the ER is dependent on ATP and sensitive to the local redox environment; folding reactions are mediated by a set of specific molecular chaperones, most of which are resident ER lumenal proteins (19,20). The best studied of these are immunoglobulin-binding protein [BiP; also known as glucose-regulated protein (grp)78], which is an ER homolog of Hsp7O, and grp94, an ER homolog of Hsp9O (19). BiP and grp94 have been shown to bind . At least in the case of BiP, the role of ATP in its chaperone funct...

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[38] Protein disulfide-isomerase

Cited by 40 publications

References 20 publications

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

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

Dual targeting of the protein disulfide isomerase RB60 to the chloroplast and the endoplasmic reticulum

Perturbations in maturation of secretory proteins and their association with endoplasmic reticulum chaperones in a cell culture model for epithelial ischemia.

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