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Università della Svizzera italiana

Division of labor among oxidoreductases : TMX1 preferentially acts on transmembrane polypeptides

Brambilla Pisoni, Giorgia ; Ruddock, Lloyd W. ; Bulleid, Neil ; Molinari, Maurizio

In: Molecular biology of the cell, 2015, vol. 26, no. 19, p. 3373-3556

The endoplasmic reticulum (ER) is the site of maturation for secretory and membrane proteins in eukaryotic cells. The lumen of the mammalian ER contains >20 members of the protein disulfide isomerase (PDI) superfamily, which ensure formation of the correct set of intramolecular and intermolecular disulfide bonds as crucial, rate-limiting reactions of the protein folding process. Components of...

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...

Università della Svizzera italiana

Stringent requirement for HRD1, SEL1L, and OS-9/XTP3-B for disposal of ERAD-LS substrates

Bernasconi, Riccardo ; Galli, Carmela ; Calanca, Verena ; Nakajima, Toshihiro ; Molinari, Maurizio

In: The journal of cell biology, 2010, vol. 188, no. 2, p. 223–235

Sophisticated quality control mechanisms prolong retention of protein-folding intermediates in the endoplasmic reticulum (ER) until maturation while sorting out terminally misfolded polypeptides for ER-associated degradation (ERAD). The presence of structural lesions in the luminal, transmembrane, or cytosolic domains determines the classification of misfolded polypeptides as ERAD-L, -M, or -C...

Università della Svizzera italiana

A selective ER‐phagy exerts procollagen quality control via a Calnexin‐FAM134B complex

Forrester, Alison ; Leonibus, Chiara De ; Grumati, Paolo ; Fasana, Elisa ; Piemontese, Marilina ; Staiano, Leopoldo ; Fregno, Ilaria ; Raimondi, Andrea ; Marazza, Alessandro ; Bruno, Gemma ; Iavazzo, Maria ; Intartaglia, Daniela ; Seczynska, Marta ; van Anken, Eelco ; Conte, Ivan ; De Matteis, Maria Antonietta ; Dikic, Ivan ; Molinari, Maurizio ; Settembre, Carmine

In: The EMBO Journal, 2019, vol. 38, no. 2, p. e99847

Autophagy is a cytosolic quality control process that recognizes substrates through receptor‐mediated mechanisms. Procollagens, the most abundant gene products in Metazoa, are synthesized in the endoplasmic reticulum (ER), and a fraction that fails to attain the native structure is cleared by autophagy. However, how autophagy selectively recognizes misfolded procollagens in the ER lumen is...

Université de Fribourg

Vectorial import via a metastable disulfide-linked complex allows for a quality control step and import by the mitochondrial disulfide relay

Habich, Markus ; Salscheider, Silja Lucia ; Murschall, Lena Maria ; Hoehne, Michaela Nicole ; Fischer, Manuel ; Schorn, Fabian ; Petrungaro, Carmelina ; Ali, Muna ; J.Erdogan, Alican ; Abou-Eid, Shadi ; Kashkar, Hamid ; Dengjel, Joern ; Riemer, Jan

In: Cell Reports, 2019, vol. 26, no. 3, p. 759-774.e5

Disulfide formation in the mitochondrial intermembrane space (IMS) is an essential process. It is catalyzed by the disulfide relay machinery, which couples substrate import and oxidation. The machinery relies on the oxidoreductase and chaperone CHCHD4-Mia40. Here, we report on the driving force for IMS import and on a redox quality control mechanism. We demonstrate that unfolded reduced...

Université de Fribourg

Spatially distinct pools of TORC1 balance protein homeostasis

Hatakeyama, Riko ; Péli-Gulli, Marie-Pierre ; Hu, Zehan ; Jaquenoud, Malika ; Osuna, Guillermo Miguel Garcia ; Sardu, Alessandro ; Dengjel, Jörn ; Virgilio, Claudio De

In: Molecular Cell, 2019, vol. 73, no. 2, p. 325-338.e8

The eukaryotic TORC1 kinase is a homeostatic controller of growth that integrates nutritional cues and mediates signals primarily from the surface of lysosomes or vacuoles. Amino acids activate TORC1 via the Rag GTPases that combine into structurally conserved multi-protein complexes such as the EGO complex (EGOC) in yeast. Here we show that Ego1, which mediates membrane-anchoring of EGOC via...

Université de Fribourg

Beyond global charge: role of amine bulkiness and protein fingerprint on nanoparticle–cell interaction

Burnand, David ; Milosevic, Ana ; Balog, Sandor ; Spuch-Calvar, Miguel ; Rothen-Rutishauser, Barbara ; Dengjel, Jörn ; Kinnear, Calum ; Moore, Thomas L. ; Petri-Fink, Alke

In: Small, 2018, vol. 14, no. 46, p. 1802088

Amino groups presented on the surface of nanoparticles are well‐known to be a predominant factor in the formation of the protein corona and subsequent cellular uptake. However, the molecular mechanism underpinning this relationship is poorly defined. This study investigates how amine type and density affect the protein corona and cellular association of gold nanoparticles with cells in...

Université de Fribourg

A conserved RxLR effector interacts with host RABA-type GTPases to inhibit vesicle-mediated secretion of antimicrobial proteins

Tomczynska, Iga ; Stumpe, Michael ; Mauch, Felix

In: The Plant Journal, 2018, vol. 95, no. 2, p. 187–203

Plant pathogens of the oomycete genus Phytophthora produce virulence factors, known as RxLR effector proteins that are transferred into host cells to suppress disease resistance. Here, we analyse the function of the highly conserved RxLR24 effector of Phytophthora brassicae. RxLR24 was expressed early in the interaction with Arabidopsis plants and ectopic expression in the host enhanced leaf...