Physical model of the nuclear membrane permeability mechanism

Minasbekyan, Liya A.; Badalyan, Hamlet G.

doi:10.1007/s12551-023-01136-8

Cited by 2 publications

(1 citation statement)

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“…Nucleoporins are a collection of around 30 distinct proteins that are assembled inside the cell to form biological "nanomachines" that form an eightfold rotationally symmetric core 8 scaffold that can expand between 40 and 60 nm in diameter [10,[16][17][18][19]22]. Nucleoporins (Nups) can be classified into three main groups based on their localization and functions: transmembrane Nups, which are integrated into the structure of the nuclear envelope (NE); central scaffold Nups, which provide structural support; and phenylalanine-glycine (FG)-Nups, which constitute the selective barrier within NPCs [4,5,9,12,[22][23][24]. Due to the varying anchoring sites of FGs, it is likely that they create distinct FG layers along the pathway via NPCs [25].…”

Section: Introductionmentioning

confidence: 99%

An Efficient Method for Isolating and Purifying Nuclei from Mice Brain for Single-Molecule Imaging Using High-Speed Atomic Force Microscopy

Qiu,

Sajidah,

Kondo

et al. 2024

Cells

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Nuclear pore complexes (NPCs) on the nuclear membrane surface have a crucial function in controlling the movement of small molecules and macromolecules between the cell nucleus and cytoplasm through their intricate core channel resembling a spiderweb with several layers. Currently, there are few methods available to accurately measure the dynamics of nuclear pores on the nuclear membranes at the nanoscale. The limitation of traditional optical imaging is due to diffraction, which prevents achieving the required resolution for observing a diverse array of organelles and proteins within cells. Super-resolution techniques have effectively addressed this constraint by enabling the observation of subcellular components on the nanoscale. Nevertheless, it is crucial to acknowledge that these methods often need the use of fixed samples. This also raises the question of how closely a static image represents the real intracellular dynamic system. High-speed atomic force microscopy (HS-AFM) is a unique technique used in the field of dynamic structural biology, enabling the study of individual molecules in motion close to their native states. Establishing a reliable and repeatable technique for imaging mammalian tissue at the nanoscale using HS-AFM remains challenging due to inadequate sample preparation. This study presents the rapid strainer microfiltration (RSM) protocol for directly preparing high-quality nuclei from the mouse brain. Subsequently, we promptly utilize HS-AFM real-time imaging and cinematography approaches to record the spatiotemporal of nuclear pore nano-dynamics from the mouse brain.

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