Thioredoxin-related transmembrane proteins : TMX1 and little brothers TMX2, TMX3, TMX4 and TMX5
- Guerra, Concetta Institute for Research in Biomedicine (IRB), Faculty of Biomedical Sciences, Università della Svizzera italiana, Switzerland
- Molinari, Maurizio Institute for Research in Biomedicine (IRB), Faculty of Biomedical Sciences, Università della Svizzera italiana, Switzerland - School of Life Sciences, École Polytechnique Fédérale de Lausanne, Switzerland
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31.08.2020
Published in:
- Cells. - 2020, vol. 9, no. 9, p. 11 p
English
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.
- Language
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- English
- Classification
- Biology, life sciences
- License
- CC BY
- Open access status
- gold
- Identifiers
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- RERO DOC 328954
- DOI 10.3390/cells9092000
- ARK ark:/12658/srd1319163
- Persistent URL
- https://n2t.net/ark:/12658/srd1319163
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