Journal
CELLS
Volume 9, Issue 9, Pages -Publisher
MDPI
DOI: 10.3390/cells9092000
Keywords
endoplasmic reticulum; ERAD; folding; PDI; TMX
Categories
Funding
- AlphaONE Foundation
- Foundation for Research on Neurodegenerative Diseases
- Swiss National Science Foundation [SNF 310030_184827]
- Comel Foundation
- Gelu Foundation
- Swiss National Science Foundation (SNF) [310030_184827] Funding Source: Swiss National Science Foundation (SNF)
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The endoplasmic reticulum (ER) is site of synthesis and maturation of membrane and secretory proteins in eukaryotic cells. The ER contains more than 20 members of the Protein Disulfide Isomerase (PDI) family. These enzymes regulate formation, isomerization and disassembly of covalent bonds between cysteine residues. As such, PDIs ensure protein folding, which is required to attain functional and transport-competent structure, and protein unfolding, which facilitates dislocation of defective gene products across the ER membrane for ER-associated degradation (ERAD). The PDI family includes over a dozen of soluble members and few membrane-bound ones. Among these latter, there are five PDIs grouped in the thioredoxin-related transmembrane (TMX) protein family. In this review, we summarize the current knowledge on TMX1, TMX2, TMX3, TMX4 and TMX5, their structural features, regulation and roles in biogenesis and control of the mammalian cell's proteome.
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