On the Impact of Post-Translational Succination on Small Ubiquitin-like Modifier 1 Structure: A Dual Approach combining Gas-Phase and Solution Studies

The conserved NUS-1/DHDDS-1 complex links N-glycosylation to lipid and lysosomal homeostasis in C. elegans.

N-glycosylation is essential for proteome integrity, yet the systemic roles of the cis-prenyltransferase (cis-PT) complex remain poorly defined. Using Caenorhabditis elegans, we demonstrate that this complex is a dual regulator of global lipid and lysosomal homeostasis. Mechanistically, NUS-1 physically associates with...

Single-molecule resolution of post-translational modification on GRK4 with cyclodextrin/SiNx hybrid nanopore.

Post-translational modifications (PTMs) on G protein-coupled receptor kinase 4 (GRK4) are implicated in hypertension pathogenesis, their label-free analysis at the single-chemical-group level remains challenging. Here, we construct a γ-cyclodextrin/silicon nitride (γ-CD/SiNx) hybrid nanopore by controlled dielectric br...

A new class of inherently efficient SUMOylation substrates

SUMOylation is an essential eukaryotic ubiquitin-like post-translational modification that plays a central role in the regulation of various nuclear processes and stress responses. It canonically occurs at lysine residues within ΨKXE consensus motifs that lie in intrinsically disordered regions or loops and interact sp...

Lysine iminylation derived from ω-3 polyunsaturated fatty acids.

Collective evidence from isotope tracing as well as genetic, dietary, and pharmacological manipulation experiments uncovered that C3-iminylation originates from cytochrome P450 (CYP)-mediated oxidation of omega-3 fatty acids, enabling further exploration of their biological and clinical implications.

Using Solution NMR to Study the RNA-Binding Properties and Molecular Mechanisms of the RNA Helicase DDX3X.

Integrated Roles of The Thioredoxin-related Protein of 14 kDa, TRP14, in Sulfur Amino Acid Metabolism, Protein Posttranslational Modifications and Signaling.

Thioredoxins and glutaredoxins are typically small "redoxin" proteins that play predominant roles in shuttling reducing power from the primary nicotinamide adenine dinucleotide phosphate (NADPH)-dependent disulfide reductases, thioredoxin reductase (TrxR, TXNRD) and glutathione disulfide-reductase (Gsr) to diverse down...