Nucleoporins: Leaving the nuclear pore complex for a successful mitosis

Chatel, Guillaume; Fahrenkrog, Birthe

doi:10.1016/j.cellsig.2011.05.023

Cited by 79 publications

(72 citation statements)

References 104 publications

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“…To minimize artifacts associated with fusion proteins targeting to sites other than NPCs, care was taken to choose subclones of cells that expressed low levels of the fusion protein. Because NPCs disassemble at mitosis, a stage when several Nups associate with other structures [notably at kinetochores in the case of Y-Nups (29,30)], cell growth was arrested for 72 h in low-serum medium before the induction of biotinylation in all of our experiments,. Immunofluorescence analyses revealed that biotinylation catalyzed by each of the BioID-Nups was largely coincident with the NPCs, as revealed by colocalization with mAb414 (which detects a subset of Nups containing FXFG repeats) (31) and anti-Nup153 ( Fig.…”

Section: Resultsmentioning

confidence: 99%

Probing nuclear pore complex architecture with proximity-dependent biotinylation

Kim

Zhu

et al. 2014

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

472

459

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Proximity-dependent biotin identification (BioID) is a method for identifying protein associations that occur in vivo. By fusing a promiscuous biotin ligase to a protein of interest expressed in living cells, BioID permits the labeling of proximate proteins during a defined labeling period. In this study we used BioID to study the human nuclear pore complex (NPC), one of the largest macromolecular assemblies in eukaryotes. Anchored within the nuclear envelope, NPCs mediate the nucleocytoplasmic trafficking of numerous cellular components. We applied BioID to constituents of the Nup107-160 complex and the Nup93 complex, two conserved NPC subcomplexes. A strikingly different set of NPC constituents was detected depending on the position of these BioID-fusion proteins within the NPC. By applying BioID to several constituents located throughout the extremely stable Nup107-160 subcomplex, we refined our understanding of this highly conserved subcomplex, in part by demonstrating a direct interaction of Nup43 with Nup85. Furthermore, by using the extremely stable Nup107-160 structure as a molecular ruler, we defined the practical labeling radius of BioID. These studies further our understanding of human NPC organization and demonstrate that BioID is a valuable tool for exploring the constituency and organization of large protein assemblies in living cells.

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Section: Resultsmentioning

confidence: 99%

Probing nuclear pore complex architecture with proximity-dependent biotinylation

Kim

Zhu

et al. 2014

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

472

459

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“…It is also possible that IQGAP3 can at least partially rescue the IQGAP1 depletion phenotype. More than 30 nucleoporins form NPCs 65 and the incomplete abscission block may be due to IQGAP1 targeting only a subset of nucleoporins. For example the nuclear envelope localization of Nup153 was not affected in IQGAP1-depleted cells during abscission, although it is required for nuclear envelope reformation and abscission.…”

Section: Discussionmentioning

confidence: 99%

IQGAP1 is associated with nuclear envelope reformation and completion of abscission

et al. 2015

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The final stage of mitosis is cytokinesis, which results in 2 independent daughter cells. Cytokinesis has 2 phases: membrane ingression followed by membrane abscission. IQGAP1 is a scaffold protein that interacts with proteins implicated in mitosis, including F-actin, myosin and CaM. IQGAP1 in yeast recruits actin and myosin II filaments to the contractile ring for membrane ingression. In contrast, we show that mammalian IQGAP1 is not required for ingression, but coordinates nuclear pore complex (NPC) reassembly and completion of abscission. Depletion of IQGAP1 disrupts Nup98 and mAb414 nuclear envelope localization and delays abscission timing. IQGAP1 phosphorylation increases 15-fold upon mitotic entry at S86, S330 and T1434, with the latter site being targeted by CDK2/Cyclin A and CDK1/Cyclin A/ B in vitro. Expressing the phospho-deficient mutant IQGAP1-S330A impairs NPC reassembly in cells undergoing abscission. Thus, mammalian IQGAP1 functions later in mitosis than its yeast counterpart to regulate nuclear pore assembly in a S330 phosphorylation-dependent manner during the abscission phase of cytokinesis.

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“…Recently, the human NDC1 protein was also reported to be essential for NPC assembly and NE formation (20,21). The NPC is a large protein complex that crosses the NE and is composed of approximately 30 nucleoporin proteins (22). NDC1 is known to interact with the nucleoporin NUP53, which is tightly associated with the nuclear membrane and physically interacts with other NPC proteins, including NUP155 (20,23).…”

Section: Discussionmentioning

confidence: 99%

A Mutation in the Nuclear Pore Complex Gene Tmem48 Causes Gametogenesis Defects in Skeletal Fusions with Sterility (sks) Mice

Akiyama¹,

Noguchi

Hirose

et al. 2013

Journal of Biological Chemistry

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Background: sks is a mouse mutant showing sterility caused by defects in meiosis. Results: We found a mutation of the Tmem48 gene encoding nuclear pore complex protein. The mutation causes aberrant splicing, resulting in deletion of an exon. Conclusion: Tmem48 is essential for meiosis and gametogenesis. Significance: This is the first report to demonstrate that the nuclear pore complex has an important role in mammalian gametogenesis.

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Nucleoporins: Leaving the nuclear pore complex for a successful mitosis

Cited by 79 publications

References 104 publications

Probing nuclear pore complex architecture with proximity-dependent biotinylation

Probing nuclear pore complex architecture with proximity-dependent biotinylation

IQGAP1 is associated with nuclear envelope reformation and completion of abscission

A Mutation in the Nuclear Pore Complex Gene Tmem48 Causes Gametogenesis Defects in Skeletal Fusions with Sterility (sks) Mice

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