<i>Saccharomyces cerevisiae MPS2</i>Encodes a Membrane Protein Localized at the Spindle Pole Body and the Nuclear Envelope

Muñoz-Centeno, Marı́a de la Cruz; McBratney, Susan; Monterrosa, Antonio; Byers, Breck; Mann, Carl; Winey, Mark

doi:10.1091/mbc.10.7.2393

Cited by 50 publications

(53 citation statements)

References 63 publications

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“…Localization was observed in wild-type cells in the absence or the presence of nocodazole and in an mps2-2 mutant at the permissive and restrictive temperatures. The mps2-2 mutant is unable to insert a duplicated SPB into the nuclear envelope and thus gives rise to cells with monopolar spindles at 37°C (47). A weak intranuclear localization was seen for Yaf9-GFP in an mps2-2 mutant at the permissive temperature of 24°C (Fig.…”

Section: Resultsmentioning

confidence: 88%

“…Mps2 (for monopolar spindle 2) is a spindle pole body (SPB) and nuclear envelope protein that is required for the insertion of the duplicated SPB into the nuclear envelope (47). We identified YNL107w as one of three genes coding for potential interacting partners of the Mps2 protein (36), the other two genes being BBP1 and SPC24 (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…We isolated Yaf9 in a two-hybrid screen with Mps2 as bait (36). Mps2 is a component of the SPB and the nuclear envelope that is required for insertion of the newly duplicated SPB into the nuclear envelope (47). It is thus necessary for establishing a normal bipolar spindle.…”

Section: Discussionmentioning

confidence: 99%

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Yaf9, a Novel NuA4 Histone Acetyltransferase Subunit, Is Required for the Cellular Response to Spindle Stress in Yeast

Masson

Jensen

et al. 2003

Molecular and Cellular Biology

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Yaf9 is one of three proteins in budding yeast containing a YEATS domain. We show that Yaf9 is part of a large complex and that it coprecipitates with three known subunits of the NuA4 histone acetyltransferase. Although Esa1, the catalytic subunit of NuA4, is essential for viability, we found that yaf9⌬ mutants are viable but hypersensitive to microtubule depolymerizing agents and synthetically lethal with two different mutants of the mitotic apparatus. Microtubules depolymerized more readily in the yaf9⌬ mutant compared to the wild type in the presence of nocodazole, and recovery of microtubule polymerization and cell division from limiting concentrations of nocodazole was inhibited. Two other NuA4 mutants (esa1-1851 and yng2⌬) and nonacetylatable histone H4 mutants were also sensitive to benomyl. Furthermore, wild-type budding yeast were more resistant to benomyl when grown in the presence of trichostatin A, a histone deacetylase inhibitor. These results strongly suggest that acetylation of histone H4 by NuA4 is required for the cellular resistance to spindle stress.

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Section: Resultsmentioning

confidence: 88%

Section: Resultsmentioning

confidence: 99%

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Yaf9, a Novel NuA4 Histone Acetyltransferase Subunit, Is Required for the Cellular Response to Spindle Stress in Yeast

Masson

Jensen

et al. 2003

Molecular and Cellular Biology

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“…Subcellular fractionation and solubilization of the P13 fraction were performed essentially as described (Munoz-Centeno et al 1999). To determine the fractionation profile of Get3, equal cell volumes were analyzed by Western blot with antibodies to GFP (Seedorf et al 1999) and Sec62.…”

Section: à5mentioning

confidence: 99%

The Conserved ATPase Get3/Arr4 Modulates the Activity of Membrane-Associated Proteins in Saccharomyces cerevisiae

et al. 2006

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The regulation of cellular membrane dynamics is crucial for maintaining proper cell growth and division. The Cdc48-Npl4-Ufd1 complex is required for several regulated membrane-associated processes as part of the ubiquitin-proteasome system, including ER-associated degradation and the control of lipid composition in yeast. In this study we report the results of a genetic screen in Saccharomyces cerevisiae for extragenic suppressors of a temperature-sensitive npl4 allele and the subsequent analysis of one suppressor, GET3/ARR4. The GET3 gene encodes an ATPase with homology to the regulatory component of the bacterial arsenic pump. Mutants of GET3 rescue several phenotypes of the npl4 mutant and transcription of GET3 is coregulated with the proteasome, illustrating a functional relationship between GET3 and NPL4 in the ubiquitin-proteasome system. We have further found that Get3 biochemically interacts with the trans-membrane domain proteins Get1/Mdm39 and Get2/Rmd7 and that Dget3 is able to suppress phenotypes of get1 and get2 mutants, including sporulation defects. In combination, our characterization of GET3 genetic and biochemical interactions with NPL4, GET1, and GET2 implicates Get3 in multiple membrane-dependent pathways.

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“…Typically, a series of 10 to 20 0.2-m optical Z-sections of cells were processed for deconvolution using nearest-neighbor algorithms and then merged to a single plane. Immuno-electron microscopy (immunoEM) was performed as described previously (12,49) using an affinity-purified rabbit polyclonal anti-GFP antibody (provided by Jason Kahana and Pam Silver) and a 5-nm gold-conjugated secondary antibody (Ted Pella, Inc.).…”

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confidence: 99%

Saccharomyces cerevisiae Mob1p Is Required for Cytokinesis and Mitotic Exit

Luca

Mody

Kurischko

et al. 2001

Molecular and Cellular Biology

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The Saccharomyces cerevisiae mitotic exit network (MEN) is a conserved set of genes that mediate the transition from mitosis to G 1 by regulating mitotic cyclin degradation and the inactivation of cyclin-dependent kinase (CDK). Here, we demonstrate that, in addition to mitotic exit, S. cerevisiae MEN gene MOB1 is required for cytokinesis and cell separation. The cytokinesis defect was evident in mob1 mutants under conditions in which there was no mitotic-exit defect. Observation of live cells showed that yeast myosin II, Myo1p, was present in the contractile ring at the bud neck but that the ring failed to contract and disassemble. The cytokinesis defect persisted for several mitotic cycles, resulting in chains of cells with correctly segregated nuclei but with uncontracted actomyosin rings. The cytokinesis proteins Cdc3p (a septin), actin, and Iqg1p/ Cyk1p (an IQGAP-like protein) appeared to correctly localize in mob1 mutants, suggesting that MOB1 functions subsequent to actomyosin ring assembly. We also examined the subcellular distribution of Mob1p during the cell cycle and found that Mob1p first localized to the spindle pole bodies during mid-anaphase and then localized to a ring at the bud neck just before and during cytokinesis. Localization of Mob1p to the bud neck required CDC3, MEN genes CDC5, CDC14, CDC15, and DBF2, and spindle pole body gene NUD1 but was independent of MYO1. The localization of Mob1p to both spindle poles was abolished in cdc15 and nud1 mutants and was perturbed in cdc5 and cdc14 mutants. These results suggest that the MEN functions during the mitosis-to-G 1 transition to control cyclin-CDK inactivation and cytokinesis.During the transition from mitosis to G 1 , cytokinesis, disassembly of the mitotic spindle, chromatin decondensation, and DNA licensing must be precisely coordinated to ensure the genomic stability and viability of the cellular progeny (22,29,31,53,67). A major signal that controls these events is the degradation of mitotic cyclins and the inactivation of cyclindependent kinase (CDK) in late mitosis (52, 68). In Saccharomyces cerevisiae, mitotic cyclin degradation and CDK inactivation are regulated by a group of genes that constitute the mitotic exit network (MEN) (45,47). MEN genes encode four protein kinases (Cdc5p, Cdc15p, Dbf2p, and Dbf20p), Cdc14p phosphatase, a GTP binding protein (Tem1p), a GTP exchange factor (Lte1p), and Mob1p, which binds Dbf2p and Dbf20p (35,36,44,57,58,73,75). At the restrictive temperature, conditional alleles of the MEN genes cause cells to arrest in late mitosis with high levels of mitotic cyclin (33,48,58,66,69). The mitotic arrest of several MEN mutants can be suppressed by overexpression of CDK inhibitor SIC1 (18, 33), indicating that CDK inactivation is the major function of the MEN pathway. Indeed, a pivotal step in cyclin and CDK inactivation is mediated by the Cdc14p phosphatase, which is sequestered in the nucleolus during most of the cell cycle until it is released at the end of mitosis (3,60,72). Release of Cdc14p from the nuc...

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Saccharomyces cerevisiae MPS2Encodes a Membrane Protein Localized at the Spindle Pole Body and the Nuclear Envelope

Cited by 50 publications

References 63 publications

Yaf9, a Novel NuA4 Histone Acetyltransferase Subunit, Is Required for the Cellular Response to Spindle Stress in Yeast

Yaf9, a Novel NuA4 Histone Acetyltransferase Subunit, Is Required for the Cellular Response to Spindle Stress in Yeast

The Conserved ATPase Get3/Arr4 Modulates the Activity of Membrane-Associated Proteins in Saccharomyces cerevisiae

Saccharomyces cerevisiae Mob1p Is Required for Cytokinesis and Mitotic Exit

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