Nuclear pore complex tethers to the cytoskeleton

Goldberg, Martin W.

doi:10.1016/j.semcdb.2017.06.017

Cited by 38 publications

(26 citation statements)

References 83 publications

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“…Thus, the translocation of late endosomes into NEI and the biogenesis of nuclear membrane folds can be two linked events involving microtubules. In addition to the presence of microtubules in NEI, microtubules running parallel to the nuclear envelope and contacting the cytoplasmic filaments of a nuclear pore complex have been observed by electron microscopy [ 174 ]. Nucleoporin proteins are indeed present in NEI containing EV-loaded Rab7 + late endosomes [ 5 ].…”

Section: Nucleoplasmic Reticulum-associated Late Endosomes: a New mentioning

confidence: 99%

Uptake and Fate of Extracellular Membrane Vesicles: Nucleoplasmic Reticulum-Associated Late Endosomes as a New Gate to Intercellular Communication

Corbeil

Santos

Karbanová

et al. 2020

Cells

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Extracellular membrane vesicles (EVs) are emerging as new vehicles in intercellular communication, but how the biological information contained in EVs is shared between cells remains elusive. Several mechanisms have been described to explain their release from donor cells and the initial step of their uptake by recipient cells, which triggers a cellular response. Yet, the intracellular routes and subcellular fate of EV content upon internalization remain poorly characterized. This is particularly true for EV-associated proteins and nucleic acids that shuttle to the nucleus of host cells. In this review, we will describe and discuss the release of EVs from donor cells, their uptake by recipient cells, and the fate of their cargoes, focusing on a novel intracellular route wherein small GTPase Rab7+ late endosomes containing endocytosed EVs enter into nuclear envelope invaginations and deliver their cargo components to the nucleoplasm of recipient cells. A tripartite protein complex composed of (VAMP)-associated protein A (VAP-A), oxysterol-binding protein (OSBP)-related protein-3 (ORP3), and Rab7 is essential for the transfer of EV-derived components to the nuclear compartment by orchestrating the particular localization of late endosomes in the nucleoplasmic reticulum.

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Section: Nucleoplasmic Reticulum-associated Late Endosomes: a New mentioning

confidence: 99%

Uptake and Fate of Extracellular Membrane Vesicles: Nucleoplasmic Reticulum-Associated Late Endosomes as a New Gate to Intercellular Communication

Corbeil

Santos

Karbanová

et al. 2020

Cells

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“…Alternative tethering mechanisms include ZYG-12–microtubule binding, which is supported by the presence of microtubule binding domains in most mammalian hook proteins (Walenta et al. , 2001), and through nuclear pore–microtubule binding, as identified in several metazoans (reviewed in Goldberg, 2017).…”

Section: Discussionmentioning

confidence: 99%

PP2A-B55/SUR-6 collaborates with the nuclear lamina for centrosome separation during mitotic entry

Boudreau

Chen

Edwards

et al. 2019

MBoC

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Across most sexually reproducing animals, centrosomes are provided to the oocyte through fertilization and must be positioned properly to establish the zygotic mitotic spindle. How centrosomes are positioned in space and time through the concerted action of key mitotic entry biochemical regulators, including protein phosphatase 2A (PP2A-B55/SUR-6), biophysical regulators, including dynein, and the nuclear lamina is unclear. Here, we uncover a role for PP2A-B55/SUR-6 in regulating centrosome separation. Mechanistically, PP2A-B55/SUR-6 regulates nuclear size before mitotic entry, in turn affecting nuclear envelope–based dynein density and motor capacity. Computational simulations predicted the requirement of PP2A-B55/SUR-6 regulation of nuclear size and nuclear-envelope dynein density for proper centrosome separation. Conversely, compromising nuclear lamina integrity led to centrosome detachment from the nuclear envelope and migration defects. Removal of PP2A-B55/SUR-6 and the nuclear lamina simultaneously further disrupted centrosome separation, leading to unseparated centrosome pairs dissociated from the nuclear envelope. Taking these combined results into consideration, we propose a model in which centrosomes migrate and are positioned through the concerted action of PP2A-B55/SUR-6–regulated nuclear envelope–based dynein pulling forces and centrosome–nuclear envelope tethering. Our results add critical precision to models of centrosome separation relative to the nucleus during spindle formation in cell division.

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“…Centrosome-nuclear envelope tethering has also been suggested to occur through ZYG-12 dimerization between outer nuclear envelope and centrosome-based pools of the hook protein (Malone et al, 2003). Alternative tethering mechanisms include ZYG-12-microtubule binding, supported by the presence of microtubule binding domains in most mammalian hook proteins (Walenta et al, 2001), as well through nuclear pore-microtubule binding, as identified in several metazoans (reviewed in Goldberg, 2017).…”

Section: Discussionmentioning

confidence: 99%

Centrosome-nuclear envelope tethering and microtubule motor-based pulling forces collaborate in centrosome positioning during mitotic entry

Boudreau

Chen

Edwards

et al. 2018

Preprint

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Centrosome positioning relative to the nucleus and cell shape is highly regulated across cell types, during cell migration and during spindle formation in cell division. Across most sexually reproducing animals, centrosomes are provided to the oocyte through fertilization and must be positioned properly to establish the zygotic mitotic spindle. How centrosomes are positioned in space and time through the concerted action of key mitotic entry biochemical regulators including Protein Phosphatase 2A (PP2A-B55/SUR-6), biophysical regulators including Dynein and the nuclear lamina is unclear. Here, we uncover a role for PP2A-B55/SUR-6 in regulating centrosome positioning. Mechanistically, PP2A-B55/SUR-6 regulates nuclear size prior to mitotic entry, in turn affecting nuclear envelope-based Dynein density and motor capacity. Using computational simulations, PP2A-B55/ SUR-6 regulation of nuclear size and nuclear envelope Dynein density were both predicted to be required for proper centrosome positioning. Conversely, compromising nuclear lamina integrity led to centrosome detachment from the nuclear envelope and migration defects. Removal of PP2A-B55/SUR-6 and the nuclear lamina simultaneously further disrupted centrosome positioning, leading to unseparated centrosome pairs dissociated from the nuclear envelope. Taken together, we propose a model in which centrosomes migrate and are positioned through the concerted action of nuclear envelope-based Dynein pulling forces and cen-trosome-nuclear envelope tethering.

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Nuclear pore complex tethers to the cytoskeleton

Cited by 38 publications

References 83 publications

Uptake and Fate of Extracellular Membrane Vesicles: Nucleoplasmic Reticulum-Associated Late Endosomes as a New Gate to Intercellular Communication

Uptake and Fate of Extracellular Membrane Vesicles: Nucleoplasmic Reticulum-Associated Late Endosomes as a New Gate to Intercellular Communication

PP2A-B55/SUR-6 collaborates with the nuclear lamina for centrosome separation during mitotic entry

Centrosome-nuclear envelope tethering and microtubule motor-based pulling forces collaborate in centrosome positioning during mitotic entry

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