Nis1 encoded by YNL078W: a new neck protein of Saccharomyces cerevisiae.

Iwase, Masayuki; Toh‐e, Akio

doi:10.1266/ggs.76.335

Cited by 33 publications

(30 citation statements)

References 34 publications

(27 reference statements)

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“…Nis1p localizes to the bud neck and interacts with the septins, which are the most abundant sumoylated proteins in the yeast cell (Iwase and Toh-e 2001). Ris1p, which has been previously implicated in silencing, contains a RING motif, suggesting that it may have E3 ligase activity (Zhang and Buchman 1997;Hannich et al 2005).…”

Section: Resultsmentioning

confidence: 99%

The Spindle Positioning Protein Kar9p Interacts With the Sumoylation Machinery in Saccharomyces cerevisiae

et al. 2008

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Accurate positioning of the mitotic spindle is important for the genetic material to be distributed evenly in dividing cells, but little is known about the mechanisms that regulate this process. Here we report that two microtubule-associated proteins important for spindle positioning interact with several proteins in the sumoylation pathway. By two-hybrid analysis, Kar9p and Bim1p interact with the yeast SUMO Smt3p, the E2 enzyme Ubc9p, an E3 Nfi1p, as well as Wss1p, a weak suppressor of a temperature-sensitive smt3 allele. The physical interaction between Kar9p and Ubc9p was confirmed by in vitro binding assays. A singleamino-acid substitution in Kar9p, L304P disrupted its two-hybrid interaction with proteins in the sumoylation pathway, but retained its interactions with the spindle positioning proteins Bim1p, Stu2p, Bik1p, and Myo2p. The kar9-L304P mutant showed defects in positioning the mitotic spindle, with the spindle located more distally than normal. Whereas wild-type Kar9p-3GFP normally localizes to only the bud-directed spindle pole body (SPB), Kar9p-L304P-3GFP was mislocalized to both SPBs. Using a reconstitution assay, Kar9p was sumoylated in vitro. We propose a model in which sumoylation regulates spindle positioning by restricting Kar9p to one SPB. These findings raise the possibility that sumoylation could regulate other microtubule-dependent processes.

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Section: Resultsmentioning

confidence: 99%

The Spindle Positioning Protein Kar9p Interacts With the Sumoylation Machinery in Saccharomyces cerevisiae

et al. 2008

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“…In our previous work, we demonstrated that Nis1 interacts with septins by two-hybrid assay using Shs1 as bait (Iwase and Toh-e, 2001). During our attempt on functional analysis of Nis1, we performed a two-hybrid screening to find the Nis1 binding proteins.…”

Section: Resultsmentioning

confidence: 99%

“…In our previous work, Nis1 was isolated by a two-hybrid screening using Shs1 as bait, and was found to be localized to the bud neck in M phase and was able to bind with all septins, Nap1, Gin4 and Kcc4 (Iwase and Toh-e, 2001). Thus, Nis1 was suggested to have some relation with the mitotic signaling network, but the exact nature of this function of Nis1 has yet to be fully elucidated.…”

Section: Introductionmentioning

confidence: 99%

Ybr267w is a New Cytoplasmic Protein Belonging to the Mitotic Signaling Network of Saccharomyces cerevisiae

Iwase

Toh‐e

2004

Cell Struct. Funct.

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ABSTRACT. YBR267w designated REI1 (required for isotropic bud growth) was isolated by two-hybrid screening using NIS1 encoding the neck protein as bait. Disruption of REI1 exhibited cold sensitive growth but did not exhibit a morphological defect. However, ∆rei1∆nap1, ∆rei1∆cla4 and ∆rei1∆gin4 double disruptants exhibited an elongated cell morphology, which was suppressed by the disruption of SWE1, indicating that REI1 is a new member of genes belonging to the mitotic signaling network that negatively regulates Swe1 kinase. ∆nap1 cells displayed a lower Gin4 kinase activity and a lower Gin4 protein level, both of which were recovered nearly to a wild type level in ∆rei1∆nap1 cells. Interaction between Rei1 and Gin4 was suggested from our observation that Rei1 inhibited Gin4 kinase activity although weakly. The facts that although ∆rei1∆nap1 cells displayed a severer elongated bud phenotype than ∆nap1 cells, Gin4 kinase activity in ∆rei1∆nap1 cells was higher than in ∆nap1 cells, and that introduction of plasmid carrying a kinase inactive gin4 mutant gene into ∆rei1∆gin4 cells suppressed their morphological defect, indicate that kinase activity of Gin4 is not required for isotropic bud growth. We found that Rei1 is localized to the cytoplasm throughout the cell cycle. In view of the fact that members belonging to the mitotic signaling network are localized to the bud neck, at least at some stage of the cell cycle, Rei1 is a unique component of this pathway.

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“…Microscopic observations were made according to the method described by Yoshida and Toh-e (2001) and Iwase and Toh-e (2001). Cells in logarithmic phase were harvested and fixed with 3.7% formalin at a room temperature for 30 minutes.…”

Section: Cytological Methodsmentioning

confidence: 99%

Genetic characterization of genes encoding enzymes catalyzing addition of phospho-ethanolamine to the glycosylphosphatidylinositol anchor in Saccharomyces cerevisiae.

Toh‐e

Oguchi

2002

Genes Genet. Syst.

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MPC1/GPI13/YLL031C , one of the genes involved in the addition of phosphoethanolamine to the glycosylphosphatidylinositol (GPI) anchor core, is an essential gene. Three available temperature-sensitive mutant alleles, mpc1-3 , mpc1-4 , and mpc1-5 , displayed different phenotypes to each other and, correspondingly, these mutants were found to have different mutations in the MPC1 ORF. Temperature-sensitivity of mpc1-5 mutants was suppressed by 5 mM ZnSO 4 and by 5 mM MnCl 2 . Multicopy suppressors were isolated from mpc1-5 mutant. Suppressors commonly effective to mpc1-4 and mpc1-5 mutations are PSD1 , encoding phosphatidylserine decarboxylase, and ECM33 , which were found to suppress the temperature-sensitive phenotype shown by the fsr2-1 and las21 ∆ mutants, those of which have defects in the GPI anchor synthesis. PSD2 , encoding another phosphatidylserine decarboxylase that is localized in Golgi/vacuole, was found to be able to serve as a multicopy suppressor of mpc1 and fsr2-1 mutants but not of the las21 ∆ mutant. In contrast to psd1 ∆ , psd2 ∆ showed a synthetic growth defect with mpc1 mutants but not with fsr2-1 or las21 ∆ . Furthermore, psd1 ∆ psd2 ∆ mpc1 triple mutants did not form colonies on nutrient medium unless ethanolamine was supplied to the medium, whereas psd1 ∆ psd2 ∆ fsr2-1 or psd1 ∆ psd2 ∆ las21 ∆ triple mutants grew on nutrient medium without supplementation of ethanolamine. These observations suggest that Mpc1 preferentially utilizes phosphatidylethanolamine produced by Psd2 that is localized in Golgi/vacuole. fsr2-1 dpl1 ∆ psd1 ∆ strains showed slower growth than fsr2-1 dpl1 ∆ psd2 ∆ , suggesting that Fsr2 enzyme depends more on Dpl1 and Psd1 for production of phosphatidylethanolamine. Las21 did not show preference for the metabolic pathway to produce phosphatidylethanolamine.

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Nis1 encoded by YNL078W: a new neck protein of Saccharomyces cerevisiae.

Cited by 33 publications

References 34 publications

The Spindle Positioning Protein Kar9p Interacts With the Sumoylation Machinery in Saccharomyces cerevisiae

The Spindle Positioning Protein Kar9p Interacts With the Sumoylation Machinery in Saccharomyces cerevisiae

Ybr267w is a New Cytoplasmic Protein Belonging to the Mitotic Signaling Network of Saccharomyces cerevisiae

Genetic characterization of genes encoding enzymes catalyzing addition of phospho-ethanolamine to the glycosylphosphatidylinositol anchor in Saccharomyces cerevisiae.

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