Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1161/01.res.24.3.361 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
The ER protein CANX (calnexin)-mediated autophagy protects against alzheimer disease.
Autophagy
January 2025
Guangdong Key Laboratory of Age-Related Cardiac and Cerebral Diseases, Department of Neurology, Affiliated Hospital of Guangdong Medical University, Zhanjiang, China.
Although the relationship between macroautophagy/autophagy and Alzheimer disease (AD) is widely studied, the underlying mechanisms are poorly understood, especially the regulatory role of the initiation signaling of autophagy on AD. Here, we find that the ER transmembrane protein CANX (calnexin) is a novel interaction partner of the autophagy-inducing kinase ULK1 and is required for ULK1 recruitment to the ER under basal or starved conditions. Loss of CANX results in the inactivity of ULK1 kinase and inhibits autophagy flux.
View Article and Find Full Text PDFInsight into the structure, oligomerization, and the role in drug resistance of human UDP-glucuronosyltransferases.
Arch Toxicol
January 2025
Department of Pharmacy, West China Hospital, Sichuan University, Chengdu, 610041, China.
Human UDP-glucuronosyltransferases (UGTs) are pivotal phase II metabolic enzymes facilitating the transfer of glucuronic acid from UDP-glucuronic acid (UDPGA) to various substrates. UGTs are classic type I transmembrane glycoproteins, mainly localized in the endoplasmic reticulum (ER) membrane. This review comprehensively explores UGTs, encompassing gene expression, functional characteristics, substrate specificity, and metabolic mechanisms.
View Article and Find Full Text PDFTanGIBLE: A selective probe for evaluating hydrophobicity-exposed defective proteins in live cells.
J Cell Biol
March 2025
Department of Biological Sciences, Laboratory of Cell Biology and Biochemistry, Tokyo Metropolitan University, Tokyo, Japan.
The accumulation of defective polypeptides in cells is a major cause of various diseases. However, probing defective proteins is difficult because no currently available method can retrieve unstable defective translational products in a soluble state. To overcome this issue, there is a need for a molecular device specific to structurally defective polypeptides.
View Article and Find Full Text PDFTranscriptomic and functional characterization of megakaryocytic-derived platelet-like particles: impaired aggregation and prominent anti-tumor effects.
Platelets
December 2025
Department of Pharmacology and Physiology, George Washington University, Washington, DC, USA.
Platelet-like particles (PLPs), derived from megakaryocytic cell lines MEG-01 and K-562, are widely used as a surrogate to study platelet formation and function. We demonstrate by RNA-Seq that PLPs are transcriptionally distinct from platelets. Expression of key genes in signaling pathways promoting platelet activation/aggregation, such as the PI3K/AKT, protein kinase A, phospholipase C, and α-adrenergic and GP6 receptor pathways, was missing or under-expressed in PLPs.
View Article and Find Full Text PDFMitoregulin self-associates to form likely homo-oligomeric pore-like complexes.
iScience
January 2025
Department of Internal Medicine, Carver College of Medicine, University of Iowa, Iowa City, IA, USA.
We and others previously found that a misannotated long noncoding RNA encodes for a conserved mitochondrial transmembrane microprotein named Mitoregulin (Mtln). Beyond an established role for Mtln in lipid metabolism, Mtln has been shown to broadly influence mitochondria, boosting respiratory efficiency and Ca retention capacity, while lowering ROS, yet the underlying mechanisms remain unresolved. Prior studies have identified possible Mtln protein interaction partners; however, a lack of consensus persists, and no claims have been made about Mtln's structure.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!