Results 61 to 70 of about 353,107 (313)

Protein pyrophosphorylation by inositol pyrophosphates — detection, function, and regulation

open access: yesFEBS Letters, EarlyView.
Protein pyrophosphorylation is an unusual signaling mechanism that was discovered two decades ago. It can be driven by inositol pyrophosphate messengers and influences various cellular processes. Herein, we summarize the research progress and challenges of this field, covering pathways found to be regulated by this posttranslational modification as ...
Sarah Lampe   +3 more
wiley   +1 more source

Ubiquitin-specific protease USP25 functions in endoplasmic reticulum-associated degradation

open access: yes, 2012
Endoplasmic Reticulum (ER)-associated degradation (ERAD) discards abnormal proteins synthesized in the ER. Through coordinated actions of ERAD components, misfolded/anomalous proteins are recognized, ubiquitinated, extracted from the ER and ultimately ...
Amanda Denuc   +14 more
core   +1 more source

UBE2O-mediated ubiquitylation directs cytoplasmic CTNNA1 to promote cell-to-ECM adhesions

open access: yesEMBO Reports
CTNNA1, a multifunctional protein that localizes at both the plasma membrane and the cytosol, plays crucial roles in actin dynamics regulation, cell-to-cell and cell-to-the extracellular matrix (ECM) adhesions and tumor suppression.
Dan Xiang   +4 more
doaj   +1 more source

SUMO-Targeted Ubiquitin Ligases (STUbLs) Reduce the Toxicity and Abnormal Transcriptional Activity Associated With a Mutant, Aggregation-Prone Fragment of Huntingtin

open access: yesFrontiers in Genetics, 2018
Cell viability and gene expression profiles are altered in cellular models of neurodegenerative disorders such as Huntington’s Disease (HD). Using the yeast model system, we show that the SUMO-targeted ubiquitin ligase (STUbL) Slx5 reduces the toxicity ...
Kentaro Ohkuni   +8 more
doaj   +1 more source

Valosin‐containing protein counteracts ATP‐driven dissolution of FUS condensates through its ATPase activity in vitro

open access: yesFEBS Letters, EarlyView.
Biomolecular condensates formed by fused in sarcoma (FUS) are dissolved by high ATP concentrations yet persist in cells. Using a reconstituted system, we demonstrate that valosin‐containing protein (VCP), an AAA+ ATPase, counteracts ATP‐driven dissolution of FUS condensates through its D2 ATPase activity.
Hitomi Kimura   +2 more
wiley   +1 more source

SUMO chain-induced dimerization activates RNF4 [PDF]

open access: yes, 2014
Dimeric RING E3 ligases interact with protein substrates and conformationally restrain the ubiquitin-E2-conjugating enzyme thioester complex such that it is primed for catalysis.
Hay, Ronald T   +5 more
core   +1 more source

Profiling Ubiquitin Chain Specificity and Topology Using Di-ubiquitin Probes

open access: yes, 2021
Ubiquitin chains of specific linkages are assembled by ubiquitin conjugating enzymes (E2s) and ubiquitin ligases (E3s) to encode unique signals in the cell.
Zhou, Han
core   +1 more source

The Roles of Ubiquitin in Mediating Autophagy

open access: yesCells, 2020
Ubiquitination, the post-translational modification essential for various intracellular processes, is implicated in multiple aspects of autophagy, the major lysosome/vacuole-dependent degradation pathway.
Zhangyuan Yin   +4 more
doaj   +1 more source

Engineering ubiquitin to modulate the ubiquitin proteosome system [PDF]

open access: yesCell Cycle, 2013
(2013). Engineering ubiquitin to modulate the ubiquitin proteosome system. Cell Cycle: Vol. 12, No. 11, pp. 1651-1652.
Andreas, Ernst, Sachdev S, Sidhu
openaire   +2 more sources

Hyperosmotic stress induces PARP1‐mediated HPF1‐dependent mono(ADP‐ribosyl)ation

open access: yesFEBS Letters, EarlyView.
Sorbitol‐induced hyperosmotic stress rapidly induces reversible mono(ADP‐ribosyl)ation (MARylation) on PARP1 without the signs of genotoxic signaling. We show that PARP1 autoMARylation is HPF1 dependent and forms hydroxylamine‐resistant O‐glycosidic linkages.
Anna Georgina Kopasz   +11 more
wiley   +1 more source

Home - About - Disclaimer - Privacy