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  Dictyostelium discoideum protein disulfide isomerase, an endoplasmic reticulum resident enzyme lacking a KDEL-type retrieval signal

Monnat, J., Hacker, U., Geissler, H., Rauchenberger, R., Neuhaus, E. M., Maniak, M., et al. (1997). Dictyostelium discoideum protein disulfide isomerase, an endoplasmic reticulum resident enzyme lacking a KDEL-type retrieval signal. FEBS Letters, 418(3), 357-362. doi:10.1016/S0014-5793(97)01415-4.

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Genre: Journal Article
Alternative Title : Dictyostelium discoideum protein disulfide isomerase, an endoplasmic reticulum resident enzyme lacking a KDEL-type retrieval signal

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FEBSLett_418_1997_357.pdf (Any fulltext), 681KB
 
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 Creators:
Monnat, Jean1, Author              
Hacker, Ulrike, Author
Geissler, Heidrun1, Author              
Rauchenberger, Robert, Author
Neuhaus, Eva Maria1, Author              
Maniak, Markus, Author
Soldati, Thierry2, Author              
Affiliations:
1Department of Molecular Cell Research, Max Planck Institute for Medical Research, Max Planck Society, ou_1497703              
2Department of Biomedical Optics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497699              

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Free keywords: Endoplasmic reticulum retrieval and retention; Protein disulfide isomerase; Dictyostelium discoideum; endoplasmic reticulum; dictyostelium discoideum; enzyme activity; protein disulfide isomerase
 Abstract: The primary activity of protein disulfide isomerase (PDI), a multifunctional resident of the endoplasmic reticulum (ER), is the isomerization of disulfide bridges during protein folding. We isolated a cDNA encoding Dictyostelium discoideum PDI (Dd-PDI). Phylogenetic analyses and basic biochemical properties indicate that it belongs to a subfamily called P5, many members of which differ from the classical PDIs in many respects. They lack an intervening inactive thioredoxin module, a C-terminal acidic domain involved in Ca2+ binding and a KDEL−type retrieval signal. Despite the absence of this motif, the ER is the steady-state location of Dd-PDI, suggesting the existence of an alternative retention mechanism for P5-related enzymes

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Language(s): eng - English
 Dates: 1997-10-271997-10-091997-10-271997-12-01
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: FEBS Letters
  Other : FEBS Lett.
Source Genre: Journal
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Publ. Info: Amsterdam : Elsevier
Pages: - Volume / Issue: 418 (3) Sequence Number: - Start / End Page: 357 - 362 Identifier: ISSN: 0014-5793
CoNE: https://pure.mpg.de/cone/journals/resource/954925399501