Brr6 drives the <i>Schizosaccharomyces pombe</i> spindle pole body nuclear envelope insertion/extrusion cycle

Tamm, Tiina; Grallert, Ágnes; Grossman, Emily P.S.; Alvarez-Tabarés, Isabel; Stevens, Frankie; Hagan, Iain

doi:10.1083/jcb.201106076

Cited by 54 publications

(71 citation statements)

References 71 publications

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“…1G). Furthermore, we were able to create gene disruptants of kms2 in vegetatively growing haploid cells, consistent with a previous study (Tamm et al, 2011). Interestingly, backcrossing a kms2-ATG::ura4 + haploid strain, in which the ura4 cassette is integrated after the start codon, leading to gene disruption, gave rise to tetrads with normal:absent colonies at a ratio of 2:2 -all viable colonies were uracil auxotrophs (Fig.…”

Section: Kms2 Is Essential After Germinationsupporting

confidence: 68%

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The KASH protein Kms2 coordinates mitotic remodeling of the spindle pole body

Wälde

King

2014

Journal of Cell Science

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Defects in the biogenesis of the spindle pole body (SPB), the yeast centrosome equivalent, can lead to monopolar spindles and mitotic catastrophe. The KASH domain protein Kms2 and the SUN domain protein Sad1 colocalize within the nuclear envelope at the site of SPB attachment during interphase and at the spindle poles during mitosis in Schizosaccharomyces pombe. We show that Kms2 interacts with the essential SPB components Cut12 and Pcp1 and the Polo kinase Plo1. Depletion of Kms2 delays mitotic entry and leads to defects in the insertion of the SPB into the nuclear envelope, disrupting stable bipolar spindle formation. These effects are mediated in part by a delay in the recruitment of Plo1 to the SPB at mitotic entry. Plo1 activity supports mitotic SPB remodeling by driving a burst of incorporation of Cut12 and Pcp1. Thus, a fission yeast SUN-KASH complex plays an important role in supporting the remodeling of the SPB at mitotic entry.

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Section: Kms2 Is Essential After Germinationsupporting

confidence: 68%

“…4F). This pattern of genetic interactions (enhancement by kms2 and suppression by kms1) is similar to those seen for an allele of brr6 that compromises mitotic SPB insertion into the nuclear envelope (Tamm et al, 2011). These findings suggest that Kms1 cannot functionally compensate for Kms2.…”

Section: Kms2 Genetically Interacts With Pcp1supporting

confidence: 51%

The KASH protein Kms2 coordinates mitotic remodeling of the spindle pole body

Wälde

King

2014

Journal of Cell Science

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“…As in the budding yeast, mutations affecting the orthologous protein of Schizosaccharomyces pombe also lead to changes in membrane properties (19). These results support the hypothesis that Brr6 and Apq12 monitor the membrane environment and coordinate the changes in the lipid composition of the NE required to maintain optimal function, thereby facilitating the construction of supramolecular protein complexes such as NPCs and SPBs (14,19,20).…”

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confidence: 73%

“…Members of the Brr6/Brl1 family of proteins are found in all fungi and lower eukaryotes that undergo closed mitosis. Whereas S. cerevisiae and many closely related fungi have both genes, S. pombe, Pneumocystis carinii, and other fungi distantly related to S. cerevisiae have a unique gene that is more closely related to Brl1 than to Brr6 (19,22). Brl1 is not a nucleoporin; its distribution in the NE is unaffected in strains carrying nucleoporin mutations that cause NPCs to cluster together (18,21).…”

mentioning

confidence: 99%

“…Both the apq12⌬ mutant and the brr6 conditional mutant are hypersensitive to drugs that inhibit lipid biosynthesis and show synthetically lethal interactions with mutations in various lipid biosynthetic pathways (14,15). As in the budding yeast, mutations affecting the orthologous protein of Schizosaccharomyces pombe also lead to changes in membrane properties (19). These results support the hypothesis that Brr6 and Apq12 monitor the membrane environment and coordinate the changes in the lipid composition of the NE required to maintain optimal function, thereby facilitating the construction of supramolecular protein complexes such as NPCs and SPBs (14,19,20).…”

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confidence: 99%

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Yeast Integral Membrane Proteins Apq12, Brl1, and Brr6 Form a Complex Important for Regulation of Membrane Homeostasis and Nuclear Pore Complex Biogenesis

et al. 2015

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bProper functioning of intracellular membranes is critical for many cellular processes. A key feature of membranes is their ability to adapt to changes in environmental conditions by adjusting their composition so as to maintain constant biophysical properties, including fluidity and flexibility. Similar changes in the biophysical properties of membranes likely occur when intracellular processes, such as vesicle formation and fusion, require dramatic changes in membrane curvature. Similar modifications must also be made when nuclear pore complexes (NPCs) are constructed within the existing nuclear membrane, as occurs during interphase in all eukaryotes. Here we report on the role of the essential nuclear envelope/endoplasmic reticulum (NE/ER) protein Brl1 in regulating the membrane composition of the NE/ER. We show that Brl1 and two other proteins characterized previously-Brr6, which is closely related to Brl1, and Apq12-function together and are required for lipid homeostasis. All three transmembrane proteins are localized to the NE and can be coprecipitated. As has been shown for mutations affecting Brr6 and Apq12, mutations in Brl1 lead to defects in lipid metabolism, increased sensitivity to drugs that inhibit enzymes involved in lipid synthesis, and strong genetic interactions with mutations affecting lipid metabolism. Mutations affecting Brl1 or Brr6 or the absence of Apq12 leads to hyperfluid membranes, because mutant cells are hypersensitive to agents that increase membrane fluidity. We suggest that the defects in nuclear pore complex biogenesis and mRNA export seen in these mutants are consequences of defects in maintaining the biophysical properties of the NE. T he nuclear envelope (NE) of eukaryotic cells compartmentalizes the nuclear material and separates it from the cytoplasm. The double membrane of the NE consists of an outer and an inner nuclear membrane (ONM and INM) that differ in protein and lipid composition. The NE is structurally and functionally related to the endoplasmic reticulum (ER), and the ONM is contiguous with the ER (1, 2). Embedded in the NE are the nuclear pore complexes (NPCs) and, in budding yeast, the spindle pole body (SPB). NPCs are extremely large and are constructed from multiple copies of about 30 different nucleoporins (nups) (3, 4). NPCs mediate selective trafficking of proteins and other macromolecules between the nucleus and the cytoplasm but also serve other important functions, including gene activation and mRNA surveillance (5, 6). The biogenesis of NPCs and their distribution over the NE are highly regulated processes and are coordinated with the cell cycle (7). During interphase, the number of NPCs doubles. In budding yeast, the NE remains intact throughout the cell cycle, and all the formation of NPCs occurs through de novo construction within the NE.In addition to the ONM and the INM, the NE contains a pore membrane domain (POM), formed by the fusion of the INM and ONM at sites where NPCs are assembled (8). The POM is a highly curved region of the NE that is i...

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The Malleable Nature of the Budding Yeast Nuclear Envelope: Flares, Fusion, and Fenestrations

Meseroll

Cohen-Fix

2016

J. Cell. Physiol.

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In eukaryotes, the nuclear envelope (NE) physically separates nuclear components and activities from rest of the cell. The NE also provides rigidity to the nucleus and contributes to chromosome organization. At the same time, the NE is highly dynamic; it must change shape and rearrange its components during development and throughout the cell cycle, and its morphology can be altered in response to mutation and disease. Here we focus on the NE of budding yeast, Saccharomyces cerevisiae, which has several unique features: it remains intact throughout the cell cycle, expands symmetrically during interphase, elongates during mitosis and, expands asymmetrically during mitotic delay. Moreover, its NE is safely breached during mating and when large structures, such as nuclear pore complexes and the spindle pole body, are embedded into its double membrane. The budding yeast NE lacks lamins and yet the nucleus is capable of maintaining a spherical shape throughout interphase. Despite these eccentricities, studies of the budding yeast NE have uncovered interesting, and likely conserved, processes that contribute to NE dynamics. In particular, we discuss the processes that drive and enable NE expansion and the dramatic changes in the NE that lead to extensions and fenestrations.

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Brr6 drives the Schizosaccharomyces pombe spindle pole body nuclear envelope insertion/extrusion cycle

Abstract: Insertion into and release of the cytoplasmic domain of the Schizosaccharomyces pombe spindle pole body from a nuclear envelope fenestra during mitosis requires Brr6.

Cited by 54 publications

References 71 publications

The KASH protein Kms2 coordinates mitotic remodeling of the spindle pole body

The KASH protein Kms2 coordinates mitotic remodeling of the spindle pole body

Yeast Integral Membrane Proteins Apq12, Brl1, and Brr6 Form a Complex Important for Regulation of Membrane Homeostasis and Nuclear Pore Complex Biogenesis

The Malleable Nature of the Budding Yeast Nuclear Envelope: Flares, Fusion, and Fenestrations

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