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

FEBS Letters

Maniak, Markus¹  Rauchenberger, Robert¹  Soldati, Thierry²  Neuhaus, Eva M.²  Hacker, Ulrike¹  Geissler, Heidrun²  Monnat, Jean² 

[1] Department of Cell Biology, Max-Planck-Institute for Biochemistry, D-82152 Martinsried, Germany;Department of Molecular Cell Research, Max-Planck-Institute for Medical Research, Jahnstrasse 29, D-69120 Heidelberg, Germany

关键词: Endoplasmic reticulum retrieval and retention;    Protein disulfide isomerase;    Dictyostelium discoideum;    ER;    endoplasmic reticulum;    PDI;    protein disulfide isomerase;   

DOI  :  10.1016/S0014-5793(97)01415-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown