Publication
The CRL5-SPSB3 ubiquitin ligase targets nuclear cGAS for degradation
Publications associées (38)
Cullin-RING ubiquitin E3 ligase regulation by the COP9 signalosome
Henning Paul-Julius Stahlberg, Simone Cavadini, Radosav Svetozara Pantelic
The cullin-RING ubiquitin E3 ligase (CRL) family comprises over 200 members in humans. The COP9 signalosome complex (CSN) regulates CRLs by removing their ubiquitin-like activator NEDD8. The CUL4A-RBX1-DDB1-DDB2 complex (CRL4A(DDB2)) monitors the genome fo ...
Springer Nature2016Ubiquitin-dependent folding of the Wnt signaling coreceptor LRP6
Françoise Gisou van der Goot Grunberg, Laurence Gouzi Abrami, Béatrice Kunz, Michal Feldman Elmalam, Elsa Anne Perrody
Many membrane proteins fold inefficiently and require the help of enzymes and chaperones. Here we reveal a novel folding assistance system that operates on membrane proteins from the cytosolic side of the endoplasmic reticulum (ER). We show that folding of ...
Elife Sciences Publications Ltd2016Five Questions (with their Answers) on ER-Associated Degradation
Production of a functional proteome is a major burden for our cells. Native proteins operate inside and outside the cells to eventually warrant life and adaptation to metabolic and environmental changes, there is no doubt that production and inappropriate ...
Wiley-Blackwell2016Scleractinian coral morphogenesis
Metamorphosis is a crucial step in the life cycle of a scleractinian coral: The swimming coral larva, the planula, settles, and metamorphoses into a sessile calcifying primary polyp, which subsequently grows into an adult colony. Importantly, morphogenesis ...
EPFL2016dRYBP Contributes to the Negative Regulation of the Drosophila Imd Pathway
The Drosophila humoral innate immune response fights infection by producing antimicrobial peptides (AMPs) through the microbe-specific activation of the Toll or the Imd signaling pathway. Upon systemic infection, the production of AMPs is both positively a ...
Public Library of Science2013Autoadaptive ER-Associated Degradation Defines a Preemptive Unfolded Protein Response Pathway
Maurizio Molinari, Riccardo Bernasconi
Folding-defective proteins must be cleared efficiently from the endoplasmic reticulum (ER) to prevent perturbation of the folding environment and to maintain cellular proteostasis. Misfolded proteins engage dislocation machineries (dislocons) built around ...
Cell Press2013Synthetic polyubiquitinated α-Synuclein reveals important insights into the roles of the ubiquitin chain in regulating its pathophysiology
Hilal Lashuel, Bruno Claude Daniel Fauvet, Mirva Hejjaoui, Mahmood Haj Yahya
Ubiquitination regulates, via different modes of modifications, a variety of biological processes, and aberrations in the process have been implicated in the pathogenesis of several neurodegenerative diseases. However, our ability to dissect the pathophysi ...
National Academy of Sciences2013Nedd4 and Nedd4-2: Ubiquitin ligases at work in the neuron
Ubiquitination of proteins by the Nedd4 family of ubiquitin ligases is a significant mechanism in protein trafficking and degradation and provides for tight spatiotemporal regulation. Ubiquitination is gaining increasing recognition as a central mechanism ...
Pergamon-Elsevier Science Ltd2013RNAi Screening Reveals Proteasome- and Cullin3-Dependent Stages in Vaccinia Virus Infection
A two-step, automated, high-throughput RNAi silencing screen was used to identify host cell factors required during vaccinia virus infection. Validation and analysis of clustered hits revealed previously unknown processes during virus entry, including a me ...
Elsevier BV2012The Size of the Proteasomal Substrate Determines Whether Its Degradation Will Be Mediated by Mono- or Polyubiquitylation
Hilal Lashuel, Mirva Hejjaoui, Mahmood Haj Yahya
A polyubiquitin chain anchored to the substrate has been the hallmark of proteasomal recognition. However, the degradation signal appears to be more complex and to contain also a substrate's unstructured region. Recent reports have shown that the proteasom ...
Cell Press2012