Toward a consensus on the mechanism of nuclear pore complex inheritance - PubMed (original) (raw)

Review

. 2014 Mar-Apr;5(2):97-102.

doi: 10.4161/nucl.28314. Epub 2014 Feb 25.

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Review

Toward a consensus on the mechanism of nuclear pore complex inheritance

C Patrick Lusk et al. Nucleus. 2014 Mar-Apr.

Abstract

Nuclear compartmentalization is achieved through the enclosure of the genome by the nuclear envelope; the nuclear envelope is perforated by nuclear pore complexes (NPCs), which form portals that control molecular exchange between the nucleus and cytoplasm. The number of NPCs per nucleus establishes a limit to the flux of molecules across the nuclear envelope and might directly impact genome organization and gene expression in a cell type specific manner. Mechanisms that control NPC number remain ill defined. Our recent study implicates a cytoplasmic pool of the nucleoporin Nsp1 as a factor that controls NPC number during the asymmetric division of budding yeast; Nsp1 acts to ensure that daughters inherit NPCs. We place our data within an emerging model of NPC inheritance in yeast and consider potential analogous mechanisms in multicellular eukaryotes, including the functional conservation of a cytoplasmic pool of Nsp1.

Keywords: actin; asymmetric division; budding yeast; diffusion barrier; nuclear envelope; nuclear pore complex; nuclear transport; nucleus.

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Figure 1. Mechanism of NPC inheritance in budding yeast. NPC dynamics and their segregation between mother and daughter cells are influenced by binding to cytoplasmic and nuclear structures including SPBs (1), and chromatin and/or chromatin binding partners like the LEM proteins (2). At least a subset of NPCs are likely attached to either a microtubule or actin-based cytoskeleton (3). There is a barrier at the bud neck (4) that impedes the passage of NPCs and other organelles, which likely responds to changes in cellular physiology. Under wild type conditions, Nsp1_CYT_ is translocated into the bud through a mechanism that requires an actin cytoskeleton and Myo2. Nsp1_CYT_ moves with ER tubules that extend from the mother nuclear envelope and contact the bud cortex; this ER might be connected to the cortex through the exocyst complex. The passage of Nsp1_CYT_ licenses NPC passage by contributing to the dissolution of the barrier (arrow). Under conditions in which there are disruptions to bud physiology and/or fitness, we propose that Nsp1_CYT_ function is inhibited, the barrier remains intact and NPCs are not transmitted.

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