Stress eating: Autophagy targets nuclear pore complexes

Gross, Angelina S.; Graef, Martin

doi:10.1083/jcb.202006007

Cited by 2 publications

(1 citation statement)

References 14 publications

(27 reference statements)

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“…Defective or unassembled Nup159-containing nucleoporin complexes are recognized by the core factor Atg8 to be directed to autophagosomes [15,16]. Nup159 thus serves as an element that controls for the integrity or function of the NPCs [15,16,63]. Additionally, Nup159 also participates in other autophagic-dependent processes, such as the Snx4-assisted vacuolar targeting of certain transcription factors [54].…”

Section: Plos Biologymentioning

confidence: 99%

Characterization of a novel interaction of the Nup159 nucleoporin with asymmetrically localized spindle pole body proteins and its link with autophagy

de Oya,

Manzano-López,

Álvarez-Llamas

et al. 2023

PLoS Biol

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Both the spindle microtubule-organizing centers and the nuclear pore complexes (NPCs) are convoluted structures where many signaling pathways converge to coordinate key events during cell division. Interestingly, despite their distinct molecular conformation and overall functions, these structures share common components and collaborate in the regulation of essential processes. We have established a new link between microtubule-organizing centers and nuclear pores in budding yeast by unveiling an interaction between the Bfa1/Bub2 complex, a mitotic exit inhibitor that localizes on the spindle pole bodies, and the Nup159 nucleoporin. Bfa1/Bub2 association with Nup159 is reduced in metaphase to not interfere with proper spindle positioning. However, their interaction is stimulated in anaphase and assists the Nup159-dependent autophagy pathway. The asymmetric localization of Bfa1/Bub2 during mitosis raises the possibility that its interaction with Nup159 could differentially promote Nup159-mediated autophagic processes, which might be relevant for the maintenance of the replicative lifespan.

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Section: Plos Biologymentioning

confidence: 99%

Characterization of a novel interaction of the Nup159 nucleoporin with asymmetrically localized spindle pole body proteins and its link with autophagy

de Oya,

Manzano-López,

Álvarez-Llamas

et al. 2023

PLoS Biol

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Nuclear envelope budding and its cellular functions

Keuenhof

Kohler

Broeskamp

et al. 2023

Nucleus

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The nuclear pore complex (NPC) has long been assumed to be the sole route across the nuclear envelope, and under normal homeostatic conditions it is indeed the main mechanism of nucleo-cytoplasmic transport. However, it has also been known that e.g. herpesviruses cross the nuclear envelope utilizing a pathway entitled nuclear egress or envelopment/de-envelopment. Despite this, a thread of observations suggests that mechanisms similar to viral egress may be transiently used also in healthy cells. It has since been proposed that mechanisms like nuclear envelope budding (NEB) can facilitate the transport of RNA granules, aggregated proteins, inner nuclear membrane proteins, and mis-assembled NPCs. Herein, we will summarize the known roles of NEB as a physiological and intrinsic cellular feature and highlight the many unanswered questions surrounding these intriguing nuclear events.

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Stress eating: Autophagy targets nuclear pore complexes

Cited by 2 publications

References 14 publications

Characterization of a novel interaction of the Nup159 nucleoporin with asymmetrically localized spindle pole body proteins and its link with autophagy

Characterization of a novel interaction of the Nup159 nucleoporin with asymmetrically localized spindle pole body proteins and its link with autophagy

Nuclear envelope budding and its cellular functions

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