Results 101 to 110 of about 232,488 (209)

Effect of Sec61 interaction with Mpd1 on endoplasmic reticulum-associated degradation.

open access: yesPLoS ONE, 2019
Proteins that misfold in the endoplasmic reticulum (ER) are transported back to the cytosol for ER-associated degradation (ERAD). The Sec61 channel is one of the candidates for the retrograde transport conduit.
Fabio Pereira   +5 more
doaj   +1 more source

Defining the Glycan Destruction Signal for Endoplasmic Reticulum-Associated Degradation [PDF]

open access: yesMolecular Cell, 2008
The endoplasmic reticulum (ER) must target potentially toxic misfolded proteins for retrotranslocation and proteasomal degradation while avoiding destruction of productive folding intermediates. For luminal proteins, this discrimination typically depends not only on the folding status of a polypeptide, but also on its glycosylation state.
Quan, Erin M.   +6 more
openaire   +2 more sources

Intercompartmental communication in senescence

open access: yesFEBS Open Bio, EarlyView.
Senescent cells experience structural changes in the plasma membrane, endoplasmic reticulum, mitochondria, lysosomes, nucleus, and cytoskeleton. These alterations disrupt crosstalk among cellular compartments, impairing vesicular trafficking, contact sites, and molecular flow.
Krystyna Mazan‐Mamczarz   +3 more
wiley   +1 more source

ER-associated degradation regulates Alzheimer’s amyloid pathology and memory function by modulating γ-secretase activity

open access: yesNature Communications, 2017
Endoplasmic-reticulum associated degradation (ERAD) regulates protein homeostasis. Here the authors identify an ERAD component membralin, and show that it interacts with a member of the γ-secretase complex to regulate β-amyloid (Aβ) pathology and memory ...
Bing Zhu   +11 more
doaj   +1 more source

Multiple Genes Core to ERAD, Macroautophagy and Lysosomal Degradation Pathways Participate in the Proteostasis Response in α1-Antitrypsin DeficiencySummary

open access: yesCellular and Molecular Gastroenterology and Hepatology
Background & Aims: In the classic form of α1-antitrypsin deficiency (ATD), the misfolded α1-antitrypsin Z (ATZ) variant accumulates in the endoplasmic reticulum (ER) of liver cells.
Jie Li   +15 more
doaj   +1 more source

SYVN1, an ERAD E3 Ubiquitin Ligase, Is Involved in GABAAα1 Degradation Associated with Methamphetamine-Induced Conditioned Place Preference

open access: yesFrontiers in Molecular Neuroscience, 2017
Abuse of methamphetamine (METH), a powerful addictive amphetamine-type stimulants (ATS), is becoming a global public health problem. The gamma-aminobutyric acid (GABA)ergic system plays a critical role in METH use disorders. By using rat METH conditioned
Dong-Liang Jiao   +12 more
doaj   +1 more source

Regulation and function of endoplasmic reticulum autophagy in neurodegenerative diseases

open access: yesNeural Regeneration Research
The endoplasmic reticulum, a key cellular organelle, regulates a wide variety of cellular activities. Endoplasmic reticulum autophagy, one of the quality control systems of the endoplasmic reticulum, plays a pivotal role in maintaining endoplasmic ...
Xiu-Yun Zhao   +5 more
doaj   +1 more source

Dexamethasone-induced selenoprotein S degradation is required for adipogenesis

open access: yesJournal of Lipid Research, 2013
Although adipogenesis is associated with induction of endoplasmic reticulum (ER) stress, the role of selenoprotein S (SEPS1), an ER resident selenoprotein known to regulate ER stress and ER-associated protein degradation, is unknown.
Choon Young Kim, Kee-Hong Kim
doaj   +1 more source

Uncoupling of p97 ATPase activity has a dominant negative effect on protein extraction [PDF]

open access: yes, 2019
p97 is a highly abundant, homohexameric AAA+ ATPase that performs a variety of essential cellular functions. Characterized as a ubiquitin-selective chaperone, p97 recognizes proteins conjugated to K48-linked polyubiquitin chains and promotes their ...
Long, David T.   +3 more
core   +1 more source

MET Suppresses Epithelial VEGFR2 via Intracrine VEGF-induced Endoplasmic Reticulum-associated Degradation

open access: yesEBioMedicine, 2015
Hepatocyte growth factor (HGF) and vascular endothelial growth factor (VEGF) drive cancer through their respective receptors, MET and VEGF receptor 2 (VEGFR2). VEGFR2 inhibits MET by promoting MET dephosphorylation.
Tom T. Chen   +7 more
doaj   +1 more source

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