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

MPS-Authors
http://pubman.mpdl.mpg.de/cone/persons/resource/persons94412

Monnat,  Jean
Department of Molecular Cell Research, Max Planck Institute for Medical Research, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons93051

Geissler,  Heidrun
Department of Molecular Cell Research, Max Planck Institute for Medical Research, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons94524

Neuhaus,  Eva Maria
Department of Molecular Cell Research, Max Planck Institute for Medical Research, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons95404

Soldati,  Thierry
Department of Biomedical Optics, Max Planck Institute for Medical Research, Max Planck Society;

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Citation

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.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0024-B9E7-F
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