Mitotic disassembly and reassembly of nuclear pore complexes

Kutay, Ulrike; Jühlen, Ramona; Antonin, Wolfram

doi:10.1016/j.tcb.2021.06.011

Cited by 65 publications

(87 citation statements)

References 127 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In actuality, the pattern of free Nups and thier complexes could vary between different cell types, tissues or organisms during mitotic disasembly. NPC reassembly would involve a "re-tying" together of Nups within the spoke at the end of telophase, which may occur upon dephosphorylation (see (79)). In the simplest model, Nic96 CTDs may associate with Nup157 and Nup170 to create the membrane interacting layer at the pore membrane (79).…”

Section: Discussionmentioning

confidence: 99%

“…NPC reassembly would involve a "re-tying" together of Nups within the spoke at the end of telophase, which may occur upon dephosphorylation (see (79)). In the simplest model, Nic96 CTDs may associate with Nup157 and Nup170 to create the membrane interacting layer at the pore membrane (79). This would provide anchor points for flexible Nic96 NTDs that connect the membrane interacting layer with the central adaptin-like layer and the inner layer, thereby guiding assembly and helping to stabilize the spoke.…”

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Comprehensive Structure and Functional Adaptations of the Yeast Nuclear Pore Complex

Akey

Singh

Ouch

et al. 2021

Preprint

View full text Add to dashboard Cite

Nuclear Pore Complexes (NPCs) mediate the nucleocytoplasmic transport of macromolecules. Here we provide a structure of the yeast NPC in which the inner ring is resolved by cryo-EM at - helical resolution to show how flexible connectors tie together different structural and functional layers in the spoke. These connectors are targets for phosphorylation and regulated disassembly in cells with an open mitosis. Moreover, some nucleoporin pairs and karyopherins have similar interaction motifs, which suggests an evolutionary and mechanistic link between assembly and transport. We also provide evidence for three major NPC variants that foreshadow functional specializations at the nuclear periphery. Cryo-electron tomography extended these studies to provide a comprehensive model of the in situ NPC with a radially-expanded inner ring. Our model reveals novel features of the central transporter and nuclear basket, suggests a role for the lumenal ring in restricting dilation and highlights the structural plasticity required for transport by the NPC.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Comprehensive Structure and Functional Adaptations of the Yeast Nuclear Pore Complex

Akey

Singh

Ouch

et al. 2021

Preprint

View full text Add to dashboard Cite

show abstract

“…Depending on whether cells break down their nuclear envelope during mitosis or not, different modes of NPC assembly exist: animal cells typically proceed via an open mitosis and disassemble the nuclear envelope, at least partially, with entry into mitosis and reassemble the nuclear envelope after successful chromatin segregation. In this mode, NPCs disassemble with the nuclear envelope at the beginning of mitosis and reassemble with the nuclear envelope during late anaphase and telophase, referred to as postmitotic or mitotic NPC assembly [ 16 ]. In addition, NPCs form de novo throughout interphase, which is hence referred to as interphase NPC assembly.…”

Section: Modes Of Npc Assemblymentioning

confidence: 99%

Dunking into the Lipid Bilayer: How Direct Membrane Binding of Nucleoporins Can Contribute to Nuclear Pore Complex Structure and Assembly

Hamed

Antonin

2021

Cells

Self Cite

View full text Add to dashboard Cite

Nuclear pore complexes (NPCs) mediate the selective and highly efficient transport between the cytoplasm and the nucleus. They are embedded in the two membrane structure of the nuclear envelope at sites where these two membranes are fused to pores. A few transmembrane proteins are an integral part of NPCs and thought to anchor these complexes in the nuclear envelope. In addition, a number of nucleoporins without membrane spanning domains interact with the pore membrane. Here we review our current knowledge of how these proteins interact with the membrane and how this interaction can contribute to NPC assembly, stability and function as well as shaping of the pore membrane.

show abstract

“…Drosophila nucleopore complex consists of ~30 different nucleoporins some of which are solubilized during early mitotic cell division (Güttinger et al, 2009;Laurell and Kutay, 2011). Nucleoporins are recruited to the chromatin in early anaphase followed by sequential reassembly of the complex (Kiseleva et al, 2001;Kutay et al, 2021). During Drosophila oogenesis, in the premeiotic stage, the GSC divides to eventually produce a 16-cell cyst (Huynh and St Johnston, 2004;Koch et al, 1967;Lehmann, 2012;Spradling et al, 2011).…”

Section: Nucleopore Complex and Heterochromatin Are In A Feedback Loop To Promote Gene Silencingmentioning

confidence: 99%

A feedback loop between heterochromatin and the nucleopore complex controls germ-cell to oocyte transition duringDrosophilaoogenesis

Sarkar

Kotb

Lemus

et al. 2021

Preprint

View full text Add to dashboard Cite

SummaryGerm cells differentiate into oocytes that become totipotent upon fertilization. How the highly specialized oocyte acquires this distinct cell fate is poorly understood. During Drosophila oogenesis, H3K9me3 histone methyltransferase SETDB1 translocates from the cytoplasm to the nucleus of germ cells concurrent with oocyte specification. Here, we discovered that nuclear SETDB1 is required to silence a cohort of differentiation-promoting genes by mediating their heterochromatinization. Intriguingly, SETDB1 is also required for the upregulation of 18 of the ~30 nucleoporins (Nups) that comprise the nucleopore complex (NPC). NPCs in turn anchor SETDB1-dependent heterochromatin at the nuclear periphery to maintain H3K9me3 and gene silencing in the egg chambers. Aberrant gene expression due to loss of SETDB1 or Nups results in loss of oocyte identity, cell death and sterility. Thus, a feedback loop between heterochromatin and NPCs promotes transcriptional reprogramming at the onset of oocyte specification that is critical to establish oocyte identity.

show abstract

Mitotic disassembly and reassembly of nuclear pore complexes

Abstract: HighlightsNPC disintegration requires the combined activity of multiple mitotic kinases and exploits multisite phosphorylation, linking it to mitotic commitment.

Cited by 65 publications

References 127 publications

Comprehensive Structure and Functional Adaptations of the Yeast Nuclear Pore Complex

Comprehensive Structure and Functional Adaptations of the Yeast Nuclear Pore Complex

Dunking into the Lipid Bilayer: How Direct Membrane Binding of Nucleoporins Can Contribute to Nuclear Pore Complex Structure and Assembly

A feedback loop between heterochromatin and the nucleopore complex controls germ-cell to oocyte transition duringDrosophilaoogenesis

Contact Info

Product

Resources

About