Quantitative regulation of nuclear pore complex proteins by O-GlcNAcylation
The nuclear pore complex (NPC) is a macromolecular assembly consisting of approximately 30 different proteins called nucleoporins. Several nucleoporins are O-GlcNAcylated, which is a post-translational modification in which the monosaccharide β-N-acetylglucosamine (GlcNAc) is attached to serine or threonine residues within proteins.
Mizuguchi-Hata, Chiaki +3 more
openaire +2 more sources
This study reveals how the mitochondrial protein Slm35 is regulated in Saccharomyces cerevisiae. The authors identify stress‐responsive DNA elements and two upstream open reading frames (uORFs) in the 5′ untranslated region of SLM35. One uORF restricts translation, and its mutation increases Slm35 protein levels and mitophagy.
Hernán Romo‐Casanueva +5 more
wiley +1 more source
A designer FG-Nup that reconstitutes the selective transport barrier of the nuclear pore complex
Intrinsically disordered FG-Nups line the Nuclear Pore Complex (NPC) lumen and form a selective barrier where transport of most proteins is inhibited, whereas specific transporter proteins are able to pass.
Alessio Fragasso +7 more
doaj +1 more source
Meiotic cellular rejuvenation is coupled to nuclear remodeling in budding yeast. [PDF]
Production of healthy gametes in meiosis relies on the quality control and proper distribution of both nuclear and cytoplasmic contents. Meiotic differentiation naturally eliminates age-induced cellular damage by an unknown mechanism.
Chetlapalli, Keerthana +6 more
core +1 more source
Comparative proteomic profiling reveals molecular characteristics associated with oogenesis and oocyte maturation during ovarian development of Bactrocera dorsalis (Hendel) [PDF]
Time-dependent expression of proteins in ovary is important to understand oogenesis in insects. Here, we profiled the proteomes of developing ovaries from Bactrocera dorsalis (Hendel) to obtain information about ovarian development with particular ...
Wei, Dong +6 more
core +1 more source
Natively Unfolded Nucleoporins Gate Protein Diffusion across the Nuclear Pore Complex [PDF]
Nuclear pore complexes (NPCs) form aqueous conduits in the nuclear envelope and gate the diffusion of large proteins between the cytoplasm and nucleoplasm. NPC proteins (nucleoporins) that contain phenylalanine-glycine motifs in filamentous, natively unfolded domains (FG domains) line the diffusion conduit of the NPC, but their role in the size ...
Patel, Samir S. +3 more
openaire +2 more sources
In situ molecular organization and heterogeneity of the Legionella Dot/Icm T4SS
We present a nearly complete in situ model of the Legionella Dot/Icm type IV secretion system, revealing its central secretion channel and identifying new components. Using cryo‐electron tomography with AI‐based modeling, our work highlights the structure, variability, and mechanism of this complex nanomachine, advancing understanding of bacterial ...
Przemysław Dutka +11 more
wiley +1 more source
Background The nuclear basket is a ‘fishtrap’-like structure on the nucleoplasmic face of the nuclear pore complex which has been implicated in diverse functions including RNA export, heterochromatin organisation, and mitosis. Recently, a novel component
Wendy A Bickmore +2 more
doaj +1 more source
Recruitment of Host Nuclear Pore Components to the Vicinity of
Parasitic protozoans of the genus Theileria are intracellular pathogens that induce the cellular transformation of leukocytes, causing uncontrolled proliferation of the infected host cell.
Sandra Huber +7 more
doaj +1 more source
Diffusion of Macromolecules across the Nuclear Pore Complex
Nuclear pore complexes (NPCs) are very selective filters that monitor the transport between the cytoplasm and the nucleoplasm. Two models have been suggested for the plug of the NPC. They are (i) it is a reversible hydrogel or (ii) it is a polymer brush.
Alber +71 more
core +1 more source

