This bud's for you: mechanisms of cellular nucleocytoplasmic trafficking via nuclear envelope budding

Fradkin, Lee G.; Budnik, Vivian

doi:10.1016/j.ceb.2016.05.001

Cited by 25 publications

(38 citation statements)

References 55 publications

(58 reference statements)

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“…We find that wash null and wash RNAi larval salivary gland nuclei exhibit an average of 0.2±0.0 (n=101) and 0.1±0.0 (n= 104) dFz2C foci/NE-buds respectively, compared to an average of 6.6±0.3 dFz2C foci/NE-buds in wildtype (n=101, p<0.0001) ( Figure 1J-L"). The phenotypes that we observe are similar to those reported previously for aPKC knockdowns (0.0±0.0, n=94, Figure 1M) (Fradkin and Budnik, 2016;Jokhi et al, 2013;Li et al, 2016;Parchure et al, 2017). TEM sections from wash null and wash RNAi knockdown nuclei showed a wrinkled nuclear membrane and a similar lack of NE-buds (n=50, n=50 respectively; Figure 1H-I).…”

Section: Wash Mutants Lack Ne-budssupporting

confidence: 90%

“…Using fluorescence and electron microscopy, biochemical and cell biological assays, and genetic perturbations in the Drosophila model, we identify Wash, its regulatory complex, and Arp2/3 as novel players in NE-budding. Surprisingly, Wash's role in this process is bipotent and, independent of Recently, Nuclear Envelope (NE-) budding was identified as an alternative pathway for nuclear exit, particularly for large developmentally-required ribonucleoprotein (megaRNP) complexes that would otherwise need to unfold/remodel to fit through the NPCs (Fradkin and Budnik, 2016;Hatch and Hetzer, 2014;Hatch and Hetzer, 2012;Jokhi et al, 2013;Li et al, 2016;Parchure et al, 2017;Speese et al, 2012). In this pathway, large macromolecule complexes, such as megaRNPs, are encircled by the nuclear lamina (type-A and type-B lamins) and inner nuclear membrane, are pinched off from the inner nuclear membrane, cross the perinuclear space, fuse with the outer nuclear membrane, and release the megaRNPs into the cytoplasm (Figure 1A-C).Strikingly, NE-budding shares many features with the nuclear egress mechanism used by herpesviruses, common pathogens that cause and/or contribute to a diverse array of human diseases (Bigalke and Heldwein, 2016;Hagen et al, 2015;Lye et al, 2017;Mettenleiter et al, 2013;Parchure et al, 2017;Roller and Baines, 2017).…”

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confidence: 99%

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Wash and the WASH Regulatory Complex function in Nuclear Envelope budding

Verboon

Nakamura

Decker

et al. 2019

Preprint

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Nuclear envelope budding is a recently described phenomenon wherein large macromolecular complexes can be packaged inside the nucleus and be extruded through the nuclear membranes, completely bypassing nuclear pores. While factors have been identified both as cargos or actively involved in this process, much remains unknown about the molecules that generate the forces and membrane deformations which appear inherent. Using fluorescence and electron microscopy, biochemical and cell biological assays, and genetic perturbations in the Drosophila model, we identify Wash, its regulatory complex, and Arp2/3 as novel players in NE-budding. Surprisingly, Wash's role in this process is bipotent and, independent of Recently, Nuclear Envelope (NE-) budding was identified as an alternative pathway for nuclear exit, particularly for large developmentally-required ribonucleoprotein (megaRNP) complexes that would otherwise need to unfold/remodel to fit through the NPCs (Fradkin and Budnik, 2016;Hatch and Hetzer, 2014;Hatch and Hetzer, 2012;Jokhi et al., 2013;Li et al., 2016;Parchure et al., 2017;Speese et al., 2012). In this pathway, large macromolecule complexes, such as megaRNPs, are encircled by the nuclear lamina (type-A and type-B lamins) and inner nuclear membrane, are pinched off from the inner nuclear membrane, cross the perinuclear space, fuse with the outer nuclear membrane, and release the megaRNPs into the cytoplasm (Figure 1A-C).Strikingly, NE-budding shares many features with the nuclear egress mechanism used by herpesviruses, common pathogens that cause and/or contribute to a diverse array of human diseases (Bigalke and Heldwein, 2016;Hagen et al., 2015;Lye et al., 2017;Mettenleiter et al., 2013;Parchure et al., 2017;Roller and Baines, 2017). As viruses often take advantage of preexisting host pathways for their livelihoods, the parallel between nuclear exit of herpesvirus nucleocapsids and that of megaRNPs suggests that NE-budding may be a general cellular mechanism that elegantly allows for the nuclear export of endogenous megaRNPs and/or other large cargos (cf. (Fradkin and Budnik, 2016;Mettenleiter et al., 2013;Parchure et al., 2017;Roller and Baines, 2017). Indeed, this pathway has also been implicated in the removal of obsolete macromolecular complexes or other material (i.e., large protein aggregates, polyubiquitylated proteins) from the nucleus (Jokhi et al., 2013;Ramaswami et al., 2013;Rose and Schlieker, 2012).The NE-budding pathway was first demonstrated in Drosophila synapse development, proving to be essential for neuromuscular junction integrity. Here, a C-terminal fragment (dFz2C) of the fly Wingless receptor, dFz2C, was shown to associate with megaRNPs that formed foci at the nuclear periphery and exited the nucleus by budding through the nuclear envelope ( Figure 1B-C) (Speese et al., 2012). Failure of this process resulted in aberrant

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Section: Wash Mutants Lack Ne-budssupporting

confidence: 90%

mentioning

confidence: 99%

Wash and the WASH Regulatory Complex function in Nuclear Envelope budding

Verboon

Nakamura

Decker

et al. 2019

Preprint

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“…New structural information on NECs together with new cryo-EM structures of capsids [46] should permit structure-guided mutational studies that should glean insight into parallels and differences between herpesvirus nucleocapsid and cellular nuclear egress processes [2,47]. …”

Section: Discussionmentioning

confidence: 99%

Getting to and through the inner nuclear membrane during herpesvirus nuclear egress

Lye

Wilkie

Filman

et al. 2017

Current Opinion in Cell Biology

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Herpesviruses, like most DNA viruses, replicate and package their genomes into capsids in the host cell nucleus. Capsids then transit to the cytoplasm in a fascinating process called nuclear egress, which includes several unusual steps: Movement of capsids from the nuclear interior to the periphery, disruption of the nuclear lamina, capsid budding through the inner nuclear membrane, and fusion of enveloped particles with the outer nuclear membrane. Here, we review recent advances and emerging questions relating to herpesvirus nuclear egress, emphasizing controversies regarding mechanisms for capsid trafficking to the nuclear periphery, and implications of recent structures of the two-subunit, viral nuclear egress complex for the process, particularly at the step of budding through the inner nuclear membrane.

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“…This unexpected discovery suggests the existence of a previously unknown pathway of myosin-driven nuclear export in plants. This pathway might complement nuclear export via the nuclear pore complex (40) and nuclear envelope budding (41). Such MadA1-mediated export might involve MadA1 attachment to material that, upon emergence from the nuclear pore complex, would bind myosin and would be rapidly trafficked through the cytosol.…”

Section: Discussionmentioning

confidence: 99%

Myosin-driven transport network in plants

Kurth

Peremyslov

Turner

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

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We investigate the myosin XI-driven transport network in Arabidopsis using protein-protein interaction, subcellular localization, gene knockout, and bioinformatics analyses. The two major groups of nodes in this network are myosins XI and their membrane-anchored receptors (MyoB) that, together, drive endomembrane trafficking and cytoplasmic streaming in the plant cells. The network shows high node connectivity and is dominated by generalists, with a smaller fraction of more specialized myosins and receptors. We show that interaction with myosins and association with motile vesicles are common properties of the MyoB family receptors. We identify previously uncharacterized myosin-binding proteins, putative myosin adaptors that belong to two unrelated families, with four members each (MadA and MadB). Surprisingly, MadA1 localizes to the nucleus and is rapidly transported to the cytoplasm, suggesting the existence of myosin XI-driven nucleocytoplasmic trafficking. In contrast, MadA2 and MadA3, as well as MadB1, partition between the cytosolic pools of motile endomembrane vesicles that colocalize with myosin XI-K and diffuse material that does not. Gene knockout analysis shows that MadB1-4 contribute to polarized root hair growth, phenocopying myosins, whereas MadA1-4 are redundant for this process. Phylogenetic analysis reveals congruent evolutionary histories of the myosin XI, MyoB, MadA, and MadB families. All these gene families emerged in green algae and show concurrent expansions via serial duplication in flowering plants. Thus, the myosin XI transport network increased in complexity and robustness concomitantly with the land colonization by flowering plants and, by inference, could have been a major contributor to this process.myosins | receptors | adaptors | cytoplasmic streaming | nuclear transport F or half of a century, it had been assumed that rapid organelle trafficking and cytoplasmic streaming in plant cells rely on myosin motors (1) and, in particular, class XI myosins that are homologous to fungal and animal class V myosins (2). Over the past decade, a massive amount of information on specific functions of myosins and mechanisms of myosin XI-dependent processes in plants has been obtained (3-5). The first genetic evidence of myosin function in cell expansion involved the demonstration of a dramatic reduction of the polarized root hair growth upon inactivation of the myosin XI-K and XI-2 genes (6, 7). Subsequently, it has been shown that myosindependent trafficking is required for the growth of multiple cell types, as well as normal plant growth and development (4,(8)(9)(10). Among the 13 paralogous myosins XI encoded in the Arabidopsis thaliana genome, the highly expressed myosins XI-K, XI-1, and XI-2 have been shown to provide the most pronounced, functionally redundant contributions to each of these processes. In contrast, another highly expressed paralog, myosin XI-I, plays only limited roles in cell and plant growth but has a specialized function in nuclear repositioning through binding nuclear e...

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This bud's for you: mechanisms of cellular nucleocytoplasmic trafficking via nuclear envelope budding

Cited by 25 publications

References 55 publications

Wash and the WASH Regulatory Complex function in Nuclear Envelope budding

Wash and the WASH Regulatory Complex function in Nuclear Envelope budding

Getting to and through the inner nuclear membrane during herpesvirus nuclear egress

Myosin-driven transport network in plants

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