Spc110p: assembly properties and role in the connection of nuclear microtubules to the yeast spindle pole body.

Kilmartin, John V.; Goh, Phuay-Yee

doi:10.1002/j.1460-2075.1996.tb00837.x

Cited by 79 publications

(93 citation statements)

References 41 publications

(56 reference statements)

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“…2). The nuclear receptor, Spc110 is a member of the pericentrin family of microtubule-nucleating proteins in which microtubule-nucleating motifs are separated from anchors by extended coiled-coil spacers (Kilmartin et al 1993;Kilmartin and Goh 1996;Sundberg and Davis 1997). These g-tubulin docking motifs are highly conserved from human pericentrin and kendrin through Drosophila centrosomin (CNN) to fission yeast Mto1 and Pcp1 (Flory et al 2002;Zhang and Megraw 2007;Fong et al 2008;Samejima et al 2008;Lin et al 2014).…”

Section: Structure and Duplication Cycle Of Yeast Spbsmentioning

confidence: 99%

The Centrosome and Its Duplication Cycle

Hagan

Glover

2015

Cold Spring Harb Perspect Biol

206

194

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Section: Structure and Duplication Cycle Of Yeast Spbsmentioning

confidence: 99%

The Centrosome and Its Duplication Cycle

Hagan

Glover

2015

Cold Spring Harb Perspect Biol

206

194

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“…To date 27 proteins have been identified, and 18 have been localized to subregions of the spindle pole (Rout and Kilmartin, 1990;Spang et al, 1996;Sundberg et al, 1996;Wigge et al, 1998). A high percentage of these proteins have predicted coiled-coil domains, including Spc42p, which forms a central crystalline core (Donaldson and Kilmartin, 1996;Bullitt et al, 1997), and Spc110p, which acts as a molecular spacer between the central and inner plaques (Kilmartin et al, 1993;Kilmartin and Goh, 1996). The amino terminus of Spc110p in turn interacts with Spc98p Sundberg and Davis, 1997;Nguyen et al, 1998), which along with Spc97p (Knopp and Schiebel, 1997) and Tub4p (Sobel and Snyder, 1995;Marschall et al, 1996;Spang et al, 1996) make up the ␥-tubulin complex at the MT ends at both the inner and outer plaques.…”

Section: Introductionmentioning

confidence: 99%

High-Voltage Electron Tomography of Spindle Pole Bodies and Early Mitotic Spindles in the YeastSaccharomyces cerevisiae

O’Toole¹,

Winey

McIntosh³

1999

MBoC

266

267

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The spindle pole body (SPB) is the major microtubule-organizing center of budding yeast and is the functional equivalent of the centrosome in higher eukaryotic cells. We used fast-frozen, freeze-substituted cells in conjunction with high-voltage electron tomography to study the fine structure of the SPB and the events of early spindle formation. Individual structures were imaged at 5-10 nm resolution in three dimensions, significantly better than can be achieved by serial section electron microscopy. The SPB is organized in distinct but coupled layers, two of which show ordered two-dimensional packing. The SPB central plaque is anchored in the nuclear envelope with hook-like structures. The minus ends of nuclear microtubules (MTs) are capped and are tethered to the SPB inner plaque, whereas the majority of MT plus ends show a distinct flaring. Unbudded cells containing a single SPB retain 16 MTs, enough to attach to each of the expected 16 chromosomes. Their median length is ϳ150 nm. MTs growing from duplicated but not separated SPBs have a median length of ϳ130 nm and interdigitate over the bridge that connects the SPBs. As a bipolar spindle is formed, the median MT length increases to ϳ300 nm and then decreases to ϳ30 nm in late anaphase. Three-dimensional models confirm that there is no conventional metaphase and that anaphase A occurs. These studies complement and extend what is known about the three-dimensional structure of the yeast mitotic spindle and further our understanding of the organization of the SPB in intact cells. INTRODUCTIONMicrotubule-organizing centers (MTOCs) nucleate and anchor microtubules (MTs) during cell differentiation and division (for review, see Brinkley, 1985;Rose et al., 1993;Kellogg et al., 1994;Pereira and Schiebel, 1997). Although MTOCs vary widely in structure, their functions are largely conserved. In metazoa, the principal MTOC is the centrosome, which organizes both the interphase MTs and those of the mitotic spindle. In the yeast Saccharomyces cerevisiae, this role is served by the spindle pole body (SPB), a complex and dynamic organelle that undergoes significant structural changes during the yeast cell cycle (for review, see Winey and Byers, 1993;Kilmartin, 1994;Snyder, 1994). Nuclear MTs, which form the meiotic or mitotic spindles, attach to an inner plaque of the SPB, whereas cytoplasmic MTs, important for nuclear movements and position, are attached to an outer plaque (Moens and Rapport, 1971;Byers and Goetsch, 1974, 1975;Rabinow and Marak, 1966). Recent studies of isolated SPBs by cryomicroscopy and electron tomography have shown that SPBs are organized from six major layers, including a central crystalline core that contains the SPC42 gene product (Bullitt et al., 1997).Duplication of the SPB during the cell cycle begins with the formation of a "satellite" on the cytoplasmic face of the half-bridge, a specialized region of the nuclear envelope that lies immediately adjacent to the existing SPB. By processes not yet described in detail, the satellite develops into a...

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“…Spc98p, Spc97p, and Tub4p interact physically and functionally (Knop et al, 1997), and all three components localize to the inner and outer plaques (Rout and Kilmartin, 1990;Spang et al, 1996a;Knop et al, 1997). Spc110p is hypothesized to connect the ␥-tubulin complex in the inner plaque to the central plaque (Kilmartin and Goh, 1996). The carboxy terminus of Spc110p, which contains a calmodulin-binding site (amino acids 897-917) (Geiser et al, 1993;Stirling et al, 1994;Spang et al, 1996b), is located at the central plaque of the SPB .…”

Section: Introductionmentioning

confidence: 99%

“…The calmodulin-Spc110p interaction is required for proper chromosome segregation (Geiser et al, 1993;Kilmartin and Goh, 1996;Stirling et al, 1996;Sundberg et al, 1996). Characterization of the carboxy-terminal temperature-sensitive allele spc110 -220, which has a mutation in the calmodulin-binding site, revealed that calmodulin binding to Spc110p is required for the proper assembly of spindle pole components.…”

Section: Introductionmentioning

confidence: 99%

“…However, the amino terminus of Spc110 -220p is apparently unaffected by the calmodulin-binding defect and remains capable of attracting nucleating components normally found at the inner plaque, thus leading to assembly of the IMO . Interestingly, the overexpression of SPC110 in wild-type cells is toxic and results in the formation of a large ordered spheroidal polymer that is composed of Spc110p and calmodulin (Kilmartin and Goh, 1996).…”

Section: Introductionmentioning

confidence: 99%

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A Mutational Analysis Identifies Three Functional Regions of the Spindle Pole Component Spc110p inSaccharomyces cerevisiae

Sundberg

Davis

1997

MBoC

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The central coiled coil of the essential spindle pole component Spc110p spans the distance between the central and inner plaques of the Saccharomyces cerevisiae spindle pole body (SPB). The carboxy terminus of Spc110p, which binds calmodulin, resides at the central plaque, and the amino terminus resides at the inner plaque from which nuclear microtubules originate. To dissect the functions of Spc110p, we created temperature-sensitive mutations in the amino and carboxy termini. Analysis of the temperature-sensitive spc110 mutations and intragenic complementation analysis of the spc110 alleles defined three functional regions of Spc110p. Region I is located at the amino terminus. Region II is located at the carboxy-terminal end of the coiled coil, and region III is the previously defined calmodulin-binding site. Overexpression of SPC98 suppresses the temperature sensitivity conferred by mutations in region I but not the phenotypes conferred by mutations in the other two regions, suggesting that the amino terminus of Spc110p is involved in an interaction with the ␥-tubulin complex composed of Spc97p, Spc98p, and Tub4p. Mutations in region II lead to loss of SPB integrity during mitosis, suggesting that this region is required for the stable attachment of Spc110p to the central plaque. Our results strongly argue that Spc110p links the ␥-tubulin complex to the central plaque of the SPB.

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Spc110p: assembly properties and role in the connection of nuclear microtubules to the yeast spindle pole body.

Cited by 79 publications

References 41 publications

The Centrosome and Its Duplication Cycle

The Centrosome and Its Duplication Cycle

High-Voltage Electron Tomography of Spindle Pole Bodies and Early Mitotic Spindles in the YeastSaccharomyces cerevisiae

A Mutational Analysis Identifies Three Functional Regions of the Spindle Pole Component Spc110p inSaccharomyces cerevisiae

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