The nucleoporins Nup170p and Nup157p are essential for nuclear pore complex assembly

Makio, Tadashi; Stanton, Leslie H.; Lin, Cheng-Chao; Goldfarb, David S.; Weis, Karsten; Wozniak, Richard W.

doi:10.1083/jcb.200810029

Cited by 80 publications

(109 citation statements)

References 82 publications

(127 reference statements)

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“…Indeed, many of these genes interact with other partially redundant nucleoporins also involved in nuclear pore complex insertion and biogenesis (e.g., NUP157 and NUP170). Furthermore, other labs have documented no obvious change in the steady-state number of nuclear pore complexes in the absence of either Nup157p or Pom152p (Madrid et al 2006;Makio et al 2009). Thus, we propose two possible models for how nucleoporin gene deletions alter the nuclear pore complex to allow compromised SPBs to more easily duplicate.…”

Section: Discussionmentioning

confidence: 99%

“…This raises the possibility that nuclear pore complexes may cause an additional type of nuclear envelope alteration that affects SPB function. Several of the nucleoporin genes that upon deletion suppress mps3 mutants code for proteins implicated in nuclear pore complex insertion or assembly, including Nup157p, Nic96p, Nup188p, Pom152p, and Pom34p (Nehrbass et al 1996;Zabel et al 1996;Gomez-Ospina et al 2000;Madrid et al 2006;Miao et al 2006;Dawson et al 2009;Flemming et al 2009;Makio et al 2009;Onischenko et al 2009). Since many of these genes are not essential for viability, while nuclear pore complexes are essential, these gene deletions are unlikely to suppress the mps3-1 defect by eliminating nuclear pore complexes or drastically reducing their number.…”

Section: Discussionmentioning

confidence: 99%

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Changes in the Nuclear Envelope Environment Affect Spindle Pole Body Duplication in Saccharomyces cerevisiae

et al. 2010

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The Saccharomyces cerevisiae nuclear membrane is part of a complex nuclear envelope environment also containing chromatin, integral and peripheral membrane proteins, and large structures such as nuclear pore complexes (NPCs) and the spindle pole body. To study how properties of the nuclear membrane affect nuclear envelope processes, we altered the nuclear membrane by deleting the SPO7 gene. We found that spo7D cells were sickened by the mutation of genes coding for spindle pole body components and that spo7D was synthetically lethal with mutations in the SUN domain gene MPS3. Mps3p is required for spindle pole body duplication and for a variety of other nuclear envelope processes. In spo7D cells, the spindle pole body defect of mps3 mutants was exacerbated, suggesting that nuclear membrane composition affects spindle pole body function. The synthetic lethality between spo7D and mps3 mutants was suppressed by deletion of specific nucleoporin genes. In fact, these gene deletions bypassed the requirement for Mps3p entirely, suggesting that under certain conditions spindle pole body duplication can occur via an Mps3p-independent pathway. These data point to an antagonistic relationship between nuclear pore complexes and the spindle pole body. We propose a model whereby nuclear pore complexes either compete with the spindle pole body for insertion into the nuclear membrane or affect spindle pole body duplication by altering the nuclear envelope environment. T HE nuclear envelope is composed of distinct outer and inner nuclear membranes. The outer nuclear membrane is continuous with the endoplasmic reticulum. The inner nuclear membrane is associated with a unique set of proteins, some of which mediate interactions between the nuclear envelope and chromatin (reviewed in Zhao et al. 2009). Nuclear pore complexes traverse both membranes and allow transport of proteins and solutes between the cytoplasm and the nucleus. The inner and outer nuclear membranes fuse in the region surrounding each nuclear pore complex.In animal cells, the nuclear envelope disassembles as cells enter mitosis and reassembles upon mitotic exit. Nuclear envelope breakdown allows the association of chromosomes with spindle microtubules, which are nucleated from centrosomes that reside in the cytoplasm. In contrast, certain types of fungi, such as the budding yeast Saccharomyces cerevisiae, undergo closed mitosis, where the nuclear envelope remains intact throughout the entire cell cycle. Closed mitosis is possible because the yeast centrosome-equivalent, the spindle pole body (SPB), is embedded in the nuclear envelope, allowing the SPB to nucleate both cytoplasmic and nuclear microtubules. SPB duplication requires a mechanism for inserting the new SPB into the nuclear envelope (reviewed in Jaspersen and Winey 2004). The new SPB begins to form in late G 1 /early S phase as satellite material deposited on the cytoplasmic face of an electron-dense region of the nuclear envelope, called the half-bridge. The satellite material matures into a dupl...

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Changes in the Nuclear Envelope Environment Affect Spindle Pole Body Duplication in Saccharomyces cerevisiae

et al. 2010

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“…[39][40][41][42] Lastly, biochemical intermediates and invaginations of the INM have been observed after the genetic imposition of assembly blocks. [43][44][45] While proteins of the reticulon family 27,28 and nups capable of deforming membranes 46,47 might generate positive membrane curvature that could help form these invaginations, it has been appropriately argued that the generation of negative curvature might be more effective in promoting the formation of a nuclear pore, 48 precisely the kind of curvature that would be compatible with an ESCRT-III mediated mechanism.…”

Section: Does Escrt-iii Directly Contribute To Npc Biogenesis?mentioning

confidence: 99%

ESCRTs breach the nuclear border

Webster

Lusk

2015

Nucleus

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T he endosomal sorting complexes required for transport (ESCRT) are best known for their role in sorting ubiquitylated membrane proteins into endosomes. The most ancient component of the ESCRT machinery is ESCRT-III, which is capable of oligomerizing into a helical filament that drives the invagination and scission of membranes aided by the AAA ATPase, Vps4, in several additional subcellular contexts. Our recent study broadens the work of ESCRT-III by identifying its role in a quality control pathway at the nuclear envelope (NE) that ensures the normal biogenesis of nuclear pore complexes (NPCs). Here, we will elaborate on how we envision this mechanism to progress and incorporate ESCRT-III into an emerging model of nuclear pore formation. Moreover, we speculate there are additional roles for the ESCRT-III machinery at the NE that broadly function to ensure its integrity and the maintenance of the nuclear compartment.

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“…A model for NPC assembly in interphase has been proposed on the basis of several studies, in which the members of the Nup93 subcomplex are first recruited to the TM-Nups (Flemming et al, 2009;Makio et al, 2009;Onischenko et al, 2009). This association, facilitated by membrane-deforming proteins (e.g.…”

Section: Assembly and Disassembly Of The Npcmentioning

confidence: 99%

The nuclear pore complex – structure and function at a glance

Kabachinski

Schwartz

2015

Journal of Cell Science

171

136

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Nuclear pore complexes (NPCs) are indispensable for cell function and are at the center of several human diseases. NPCs provide access to the nucleus and regulate the transport of proteins and RNA across the nuclear envelope. They are aqueous channels generated from a complex network of evolutionarily conserved proteins known as nucleporins. In this Cell Science at a Glance article and the accompanying poster, we discuss how transport between the nucleoplasm and the cytoplasm is regulated, what we currently know about the structure of individual nucleoporins and the assembled NPC, and how the cell regulates assembly and disassembly of such a massive structure. Our aim is to provide a general overview on what we currently know about the nuclear pore and point out directions of research this area is heading to.

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The nucleoporins Nup170p and Nup157p are essential for nuclear pore complex assembly

Cited by 80 publications

References 82 publications

Changes in the Nuclear Envelope Environment Affect Spindle Pole Body Duplication in Saccharomyces cerevisiae

Changes in the Nuclear Envelope Environment Affect Spindle Pole Body Duplication in Saccharomyces cerevisiae

ESCRTs breach the nuclear border

The nuclear pore complex – structure and function at a glance

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