Ubiquitylation of the nuclear pore complex controls nuclear migration during mitosis in <i>S. cerevisiae</i>

Hayakawa, Akira; Babour, Anna; Sengmanivong, Lucie; Dargemont, Catherine

doi:10.1083/jcb.201108124

Cited by 45 publications

(54 citation statements)

References 35 publications

(48 reference statements)

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“…Ubiquitylation of Nup159 at Lys-897 N-terminal to the Dyn2 recognition motifs appears to control the anchoring of Dyn2 to the nuclear pore complex (43). Although it is clear that binding of Dyn2 does not require ubiquitylation of Nup159 (this work and Ref.…”

Section: The Did Domain Of Nup159 Is Intrinsically Disordered With Inmentioning

confidence: 75%

Multiple Recognition Motifs in Nucleoporin Nup159 Provide a Stable and Rigid Nup159-Dyn2 Assembly

Nyarko

Song

Nováček

et al. 2013

Journal of Biological Chemistry

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Background: Nucleoporin Nup159 has multiple recognition motifs for Dyn2, the yeast ortholog of LC8. Results: Nup159 is intrinsically disordered and binds Dyn2 cooperatively at five of the six recognition motifs. Conclusion: Initial binding aligns two Nup chains in a bivalent scaffold; motifs 5 and 6 underlie rigidity. Significance: Multiple recognition sites provide entropy/enthalpy balance to a stable yet entropically unfavorable rigid complex.

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Section: The Did Domain Of Nup159 Is Intrinsically Disordered With Inmentioning

confidence: 75%

Multiple Recognition Motifs in Nucleoporin Nup159 Provide a Stable and Rigid Nup159-Dyn2 Assembly

Nyarko

Song

Nováček

et al. 2013

Journal of Biological Chemistry

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“…95 Prevalence of monoubiquitination and involvement of distinct components of the ubiquitin conjugation machinery suggest that ubiquitination of the Nups is not only connected to proteasome-dependent protein degradation but rather associated with regulation of the NPC function. 95 Some nucleoporins have been postulated to be ubiquitinated by Rsp5 in vitro, e.g., Nup2, Nup60, Nup116, Nup192, while the proposed ubiquitination of others was not confirmed in vivo, e.g., Nup1, Nup42, Nup49 (Table 1). For Nup159, postulated to be ubiquitinated by Rsp5 in vitro, another ligase was identified in vivo (Table 1).…”

Section: Discussionmentioning

confidence: 99%

Role of Rsp5 ubiquitin ligase in biogenesis of rRNA, mRNA and tRNA in yeast

Domanska

Kamińska

2015

RNA Biology

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Rsp5 ubiquitin ligase is required for ubiquitination of a wide variety of proteins involved in essential processes. Rsp5 was shown to be involved in regulation of lipid biosynthesis, intracellular trafficking of proteins, response to various stresses, and many other processes. In this article, we provide a comprehensive review of the nuclear and cytoplasmic functions of Rsp5 with a focus on biogenesis of different RNAs. We also briefly describe the participation of Rsp5 in the regulation of the RNA polymerase II complex, and its potential role in the regulation of other RNA polymerases. Moreover, we emphasize the function of Rsp5 in the coordination of the different steps of rRNA, mRNA and tRNA metabolism in the context of protein biosynthesis. Finally, we highlight the involvement of Rsp5 in controlling diverse cellular mechanisms at multiple levels and in adaptation of the cell to changing growth conditions.

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“…As observed with fluorescence and confirmed with structured illuminated microscopy (SIM), LGN concentrated into bright discrete structures at the NPC that colocalized with another integral component of NPC fused to a red variant, Nup159-mCherry ( Fig. 3; Hayakawa et al, 2012). Interestingly, the nuclear envelope exhibited important deformations, with elongated structures reminiscent of those observed in an Δndj1 mutant during meiotic prophase, where subtelomeres are detached from the LINC complex, but actin cables keep pulling on the nuclear envelope external membrane, leading to nuclear envelope deformations .…”

mentioning

confidence: 92%

Evidence for actin dual role in regulating chromosome organization and dynamics in yeast

Spichal

Brion

Herbert

et al. 2016

Journal of Cell Science

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Eukaryotic chromosomes undergo movements that are involved in the regulation of functional processes such as DNA repair. To better understand the origin of these movements, we used fluorescence microscopy, image analysis and chromosome conformation capture to quantify the actin contribution to chromosome movements and interactions in budding yeast. We show that both the cytoskeletal and nuclear actin drive local chromosome movements, independently of Csm4, a putative LINC protein. Inhibition of actin polymerization reduces subtelomere dynamics, resulting in more confined territories and enrichment in subtelomeric contacts. Artificial tethering of actin to nuclear pores increased both nuclear pore complex (NPC) and subtelomere motion. Chromosome loci that were positioned away from telomeres exhibited reduced motion in the presence of an actin polymerization inhibitor but were unaffected by the lack of Csm4. We further show that actin was required for locus mobility that was induced by targeting the chromatin-remodeling protein Ino80. Correlated with this, DNA repair by homologous recombination was less efficient. Overall, interphase chromosome dynamics are modulated by the additive effects of cytoskeletal actin through forces mediated by the nuclear envelope and nuclear actin, probably through the function of actin in chromatin-remodeling complexes.

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Ubiquitylation of the nuclear pore complex controls nuclear migration during mitosis in S. cerevisiae

Abstract: A systematic analysis revealed that the nuclear pore complex is extensively modified by ubiquitin and that ubiquitylation of the NPC component Nup159 is required for dynein light chain targeting to the NPC and proper nuclear segregation during mitosis.

Cited by 45 publications

References 35 publications

Multiple Recognition Motifs in Nucleoporin Nup159 Provide a Stable and Rigid Nup159-Dyn2 Assembly

Multiple Recognition Motifs in Nucleoporin Nup159 Provide a Stable and Rigid Nup159-Dyn2 Assembly

Role of Rsp5 ubiquitin ligase in biogenesis of rRNA, mRNA and tRNA in yeast

Evidence for actin dual role in regulating chromosome organization and dynamics in yeast

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