Removal of a Single Pore Subcomplex Results in Vertebrate Nuclei Devoid of Nuclear Pores

Harel, Amnon; Orjalo, Arturo V.; Vincent, Thomas M.; Lachish-Zalait, Aurélie; Vasu, Sanjay; Shah, Sundeep; Zimmerman, Ella; Elbaum, Michael; Forbes, Douglass J.

doi:10.1016/s1097-2765(03)00116-3

Cited by 258 publications

(310 citation statements)

References 65 publications

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“…Such a study previously revealed that partial depletion of Nup133, Nup107, or Nup85 leads to the decreased localization of several nucleoporins at the nuclear envelope (Boehmer et al, 2003;Harel et al, 2003;Walther et al, 2003a). We could further correlate this decreased labeling to an overall decrease of NPC number in the Nup133 or Nup107-depleted cells (Walther et al, 2003a).…”

Section: Rna Interference Of Seh1 Induces Phenotypes Similar To Nup13mentioning

confidence: 52%

“…So far, three constituents of the Nup107-160 complex, Nup133, Nup107, and Nup85, have been localized to kinetochores in mitosis (Belgareh et al, 2001;Harel et al, 2003). Because those results suggested that the entire Nup107-160 complex might be targeted to kinetochores in mitosis, we analyzed the localization of GFP-tagged constituents of this complex in mitotic HeLa cells.…”

Section: Gfp-tagging Reveals the Association Of Nup160 Nup37 Nup43mentioning

confidence: 99%

“…RNA interference approaches in Caenorhabditis elegans early embryo and HeLa cells further revealed the involvement of RanBP2/ Nup358 in chromosome congression and segregation, stable kinetochore-microtubule association, and kinetochore assembly (Askjaer et al, 2002;Salina et al, 2003;Joseph et al, 2004). Finally, a fraction of human Nup133, Nup107, and Nup85/75 was shown to associate with kinetochores in mitosis (Belgareh et al, 2001;Harel et al, 2003).…”

Section: Introductionmentioning

confidence: 98%

“…This complex was shown to be involved in NPC distribution in S. cerevisiae, and in mRNA export both in yeast (reviewed in Doye and Hurt, 1997) and vertebrates (Vasu et al, 2001;Boehmer et al, 2003;Walther et al, 2003a). More recently, this complex was demonstrated to also be critical for NPC assembly in vertebrates (Harel et al, 2003;Walther et al, 2003a).…”

Section: Introductionmentioning

confidence: 99%

“…Isolation under native conditions and in vitro reconstitution have further revealed the Y-shaped structure of this complex (Siniossoglou et al, 2000;Lutzmann et al, 2002). The vertebrate Nup107-160 complex was so far demonstrated to consist of Nup107 (homologous to ScNup84), Nup133 (homologous to ScNup133), Nup160 (homologous to ScNup120 and thus also referred in human cells as Nup120), Nup96 (homologous to ScNup145-C), Sec13 and Nup85/75 (Fontoura et al, 1999;Belgareh et al, 2001;Vasu et al, 2001;Harel et al, 2003). In addition, previous studies reported the cofractionation on sucrose gradients of Nup107, Nup96, and Sec13 together with a 37-kDa WD-repeat containing protein (Fontoura et al, 1999), subsequently identified as Nup37 (Cronshaw et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

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The Entire Nup107-160 Complex, Including Three New Members, Is Targeted as One Entity to Kinetochores in Mitosis

Loïodice

Alves

Rabut

et al. 2004

MBoC

254

240

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In eukaryotes, bidirectional transport of macromolecules between the cytoplasm and the nucleus occurs through elaborate supramolecular structures embedded in the nuclear envelope, the nuclear pore complexes (NPCs). NPCs are composed of multiple copies of ϳ30 different proteins termed nucleoporins, of which several can be biochemically isolated as subcomplexes. One such building block of the NPC, termed the Nup107-160 complex in vertebrates, was so far demonstrated to be composed of six different nucleoporins. Here, we identify three WD (Trp-Asp)-repeat nucleoporins as new members of this complex, two of which, Nup37 and Nup43, are specific to higher eukaryotes. The third new member Seh1 is more loosely associated with the Nup107-160 complex biochemically, but its depletion by RNA interference leads to phenotypes similar to knock down of other constituents of this complex. By combining green fluorescent protein-tagged nucleoporins and specific antibodies, we show that all the constituents of this complex, including Nup37, Nup43, Seh1, and Sec13, are targeted to kinetochores from prophase to anaphase of mitosis. Together, our results indicate that the entire Nup107-160 complex, which comprises nearly one-third of the so-far identified nucleoporins, specifically localizes to kinetochores in mitosis.

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Section: Rna Interference Of Seh1 Induces Phenotypes Similar To Nup13mentioning

confidence: 52%

Section: Gfp-tagging Reveals the Association Of Nup160 Nup37 Nup43mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

The Entire Nup107-160 Complex, Including Three New Members, Is Targeted as One Entity to Kinetochores in Mitosis

Loïodice

Alves

Rabut

et al. 2004

MBoC

254

240

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Puzzling out nuclear pore complex assembly

Penzo,

Palancade

2023

FEBS Letters

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Nuclear pore complexes (NPCs) are sophisticated multiprotein assemblies embedded within the nuclear envelope and controlling the exchanges of molecules between the cytoplasm and the nucleus. In this review, we summarize the mechanisms by which these elaborate complexes are built from their subunits, the nucleoporins, based on our ever‐growing knowledge of NPC structural organization and on the recent identification of additional features of this process. We present the constraints faced during the production of nucleoporins, their gathering into oligomeric complexes, and the formation of NPCs within nuclear envelopes, and review the cellular strategies at play, from co‐translational assembly to the enrolment of a panel of cofactors. Remarkably, the study of NPCs can inform our perception of the biogenesis of multiprotein complexes in general – and vice versa.

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The Nuclear Pore Complex and Nuclear Transport

Zagairy

Fichtman

Harel

2015

Encyclopedia of Life Sciences

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The nuclear pore complex (NPC) is an essential gateway between the cell nucleus and the cytoplasm. The NPC is formed by multiple copies of ∼30 different proteins called nucleoporins, which can be divided into scaffold, membrane‐anchored and barrier components. Thousands of phenylalanine‐glycine (FG) repeats, found in barrier nucleoporins, interact to form the selective permeability barrier of the NPC channel. Shuttling nuclear transport receptors are able to interact with these FG repeats and mediate the passage of large macromolecular cargoes through the barrier. Combinations of shuttling receptors, their adaptors and localisation signals in cargo molecules define a wide array of nuclear import and export pathways. Recent research has pointed to some dynamic features in NPC components, as well as a number of nucleoporin‐related human diseases which are characterised by highly cell‐type‐specific phenotypes. Key Concepts The nuclear pore complex (NPC) is a massive and elaborate structure formed by multiple copies of ∼30 different nucleoporins. The selective permeability barrier of the NPC is formed by hydrophobic interactions among FG repeats found in a large group of nucleoporins. Ions and small molecules are able to passively diffuse through the aqueous central channel of the NPC. Macromolecules transported through the NPC must contain specific targeting signals for nuclear import and nuclear export. Targeting signals are recognised by shuttling transport receptors which mediate the passage through the NPC channel by interacting with FG repeats. A small number of inherited diseases have been linked to mutations in human nucleoporins and are characterised by cell‐type‐specific phenotypes.

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Removal of a Single Pore Subcomplex Results in Vertebrate Nuclei Devoid of Nuclear Pores

Cited by 258 publications

References 65 publications

The Entire Nup107-160 Complex, Including Three New Members, Is Targeted as One Entity to Kinetochores in Mitosis

The Entire Nup107-160 Complex, Including Three New Members, Is Targeted as One Entity to Kinetochores in Mitosis

Puzzling out nuclear pore complex assembly

The Nuclear Pore Complex and Nuclear Transport

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