Results 81 to 90 of about 6,849 (214)
Nuclear Pore Complexes (NPCs) are embedded in the nuclear envelope (NE), regulating macromolecule transport and physically interacting with chromatin. The NE undergoes dramatic breakdown and reformation during plant cell division.
Martinez-Garcia, Marina +5 more
core +1 more source
Cytoplasmic nucleoporin assemblage: the cellular artwork in physiology and disease
Nucleoporins, essential proteins building the nuclear pore, are pivotal for ensuring nucleocytoplasmic transport. While traditionally confined to the nuclear envelope, emerging evidence indicates their presence in various cytoplasmic structures ...
Junyan Lin, Izabela Sumara
doaj +1 more source
Identification of Yeast Protein Sequences With Similarity to the ESCRT‐III Protein Snf7
ABSTRACT Endosomal sorting complex required for transport (ESCRT‐III) is a membrane remodeling complex involved in a large number of cellular processes. It appears to perform an essential function in eukaryotes, since to date no eukaryotic organism completely devoid of ESCRT‐III has been found.
Thomas Brune, Ralf Kölling
wiley +1 more source
Functional insights of nucleocytoplasmic transport in plants
Plant nucleocytoplasmic transport beyond the nuclear envelope is important not only for basic cellular functions but also for growth, development, hormonal signalling, and responses to environmental stimuli.
Kentaro eTamura, Ikuko eHara-Nishimura
doaj +1 more source
As we age, cells gradually accumulate damage, which can contribute to disease and neurodegeneration. This review explores how two cellular recycling processes, mitophagy and nucleophagy, remove damaged mitochondria and nuclear material, respectively, to maintain cell health and long‐term neuronal homeostasis.
Maria Markaki, Nektarios Tavernarakis
wiley +1 more source
Two structurally distinct domains of the nucleoporin Nup170 cooperate to tether a subset of nucleoporins to nuclear pores [PDF]
How individual nucleoporins (Nups) perform their role in nuclear pore structure and function is largely unknown. In this study, we examined the structure of purified Nup170 to obtain clues about its function. We show that Nup170 adopts a crescent moon shape with two structurally distinct and separable domains, a β-propeller N terminus and an α-solenoid
Flemming, Dirk +5 more
openaire +3 more sources
ABSTRACT The cytosolic iron–sulfur (Fe‐S) cluster assembly (CIA) targeting complex mediates the maturation of cytosolic and nuclear Fe‐S proteins and governs core eukaryotic cellular processes. However, whether this complex contributes to plant disease resistance remains unclear.
Huanbin Shi +10 more
wiley +1 more source
Co-translational assembly orchestrates competing biogenesis pathways
The biogenesis of nuclear pores imposes a logistic challenge for cells. Here, the authors investigate structural motifs for co-translational interactions in nucleoporins and find that co-translational assembly events differ between paralogous assembly ...
Maximilian Seidel +14 more
doaj +1 more source
Photoperiodic flowering is well studied in facultative photoperiodism plants, but the genetic basis of obligate photoperiodism remains poorly understood. Using QTL mapping and RNA‐seq in Mimulus guttatus, we identified photoperiodism‐specific QTLs that are distinct from flowering‐time QTLs, supporting switch‐like genetic control of obligate long‐day ...
Po‐Kai Huang, Daniel E. Runcie
wiley +1 more source
The Multiple Faces of Disordered Nucleoporins
An evolutionary advantage of intrinsically disordered proteins (IDPs) is their ability to bind a variety of folded proteins-a paradigm that is central to the nucleocytoplasmic transport mechanism, in which nuclear transport receptors mediate the translocation of various cargo through the nuclear pore complex by binding disordered phenylalanine-glycine ...
openaire +2 more sources

