Università della Svizzera italiana

Thioredoxin-related transmembrane proteins : TMX1 and little brothers TMX2, TMX3, TMX4 and TMX5

Guerra, Concetta ; Molinari, Maurizio

In: Cells, 2020, vol. 9, no. 9, p. 11 p

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...

Università della Svizzera italiana

Proteasomal and lysosomal clearance of faulty secretory proteins : ER-associated degradation (ERAD) and ER-to-lysosome-associated degradation (ERLAD) pathways

Fregno, Ilaria ; Molinari, Maurizio

In: Critical reviews in biochemistry and molecular biology, 2019, vol. 54, no. 2, p. 153-163

About 40% of the eukaryotic cell’s proteins are inserted co- or post-translationally in the endoplasmic reticulum (ER), where they attain the native structure under the assistance of resident molecular chaperones and folding enzymes. Subsequently, these proteins are secreted from cells or are transported to their sites of function at the plasma membrane or in organelles of the secretory and ...

Università della Svizzera italiana

ESCRT-III-driven piecemeal micro-ER-phagy remodels the ER during recovery from ER stress

Loi, Marisa ; Raimondi, Andrea ; Morone, Diego ; Molinari, Maurizio

In: Nature communications, 2019, vol. 10, p. 5058

The endoplasmic reticulum (ER) produces about 40% of the nucleated cell’s proteome. ER size and content in molecular chaperones increase upon physiologic and pathologic stresses on activation of unfolded protein responses (UPR). On stress resolution, the mammalian ER is remodeled to pre-stress, physiologic size and function on activation of the LC3-binding activity of the translocon...

Università della Svizzera italiana

Proteostasis : bad news and good news from the endoplasmic reticulum

Noack, Julia ; Brambilla Pisoni, Giorgia ; Molinari, Maurizio

In: Swiss medical weekly, 2014, vol. 144, p. w14001

The endoplasmic reticulum (ER) is an intracellular compartment dedicated to the synthesis and maturation of secretory and membrane proteins, totalling about 30% of the total eukaryotic cells proteome. The capacity to produce correctly folded polypeptides and to transport them to their correct intra- or extracellular destinations relies on proteostasis networks that regulate and balance the...

Università della Svizzera italiana

UDP-glucose : glycoprotein glucosyltransferase (UGGT1) promotes substrate solubility in the endoplasmic reticulum

Ferris, Sean P. ; Jaber, Nikita S. ; Molinari, Maurizio ; Arvan, Peter ; Kaufman, Randal J.

In: Molecular biology of the cell, 2013, vol. 24, no. 17, p. 2597-2608

Protein folding in the endoplasmic reticulum (ER) is error prone, and ER quality control (ERQC) processes ensure that only correctly folded proteins are exported from the ER. Glycoproteins can be retained in the ER by ERQC, and this retention contributes to multiple human diseases, termed ER storage diseases. UDP- glucose:glycoprotein glucosyltransferase (UGGT1) acts as a central component of...