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Article

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

The EMBO journal - 2 Sept 1996

Kilmartin J V, Goh P Y

Abstract excerpt

Spc110p is an essential component of the budding yeast spindle pole body (SPB). It binds calmodulin and contains a long central coiled-coil rod which acts as a spacer element between the central plaque of the SPB and the ends of the nuclear or spindle microtubules. This suggests that the essentia...

Topics

Binding Sites
Calmodulin
Calmodulin-Binding Proteins
Cell Nucleus
Cytoskeletal Proteins
Fungal Proteins
Microscopy, Immunoelectron
Microtubules
Mutation
Nuclear Proteins
Phenotype
Saccharomyces cerevisiae

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Saccharomyces cerevisiae Proteins

Spindle Apparatus

Source

Open in PubMed Open full text

Identifiers

PMID: 8887551
PMCID: PMC452189

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026. Prepared record publication-8887551-2026-08-30.1. Manifest publication-graph-cohort-2026-08-30.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 30 Aug 2026.

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Spc110p: assembly properties and role in the connection of nuclear microtubules to the yeast spindle pole body.PMID 8887551Read ↗

Role of calmodulin and Spc110p interaction in the proper assembly of spindle pole body compenents.Semantic proximity Read ↗

A mutational analysis identifies three functional regions of the spindle pole component Spc110p in Saccharomyces cerevisiae.Semantic proximity Read ↗

Analysis of a spindle pole body mutant reveals a defect in biorientation and illuminates spindle forces.Semantic proximity Read ↗

A genetic analysis of interactions with Spc110p reveals distinct functions of Spc97p and Spc98p, components of the yeast gamma-tubulin complex.Semantic proximity Read ↗

Mutations which block the binding of calmodulin to Spc110p cause multiple mitotic defects.Semantic proximity Read ↗

Mutations in SPC110, encoding the yeast spindle pole body calmodulin-binding protein, cause defects in cell integrity as well as spindle formation.Semantic proximity Read ↗

Spc42p: a phosphorylated component of the S. cerevisiae spindle pole body (SPD) with an essential function during SPB duplication.Semantic proximity Read ↗

Interaction with calmodulin is required for the function of Spc110p, an essential component of the yeast spindle pole body.Semantic proximity Read ↗

Characterization of spindle pole body duplication reveals a regulatory role for nuclear pore complexes.Semantic proximity Read ↗

The nuclear pore complex-associated protein, Mlp2p, binds to the yeast spindle pole body and promotes its efficient assembly.Semantic proximity Read ↗

The spindle pole body component Spc97p interacts with the gamma-tubulin of Saccharomyces cerevisiae and functions in microtubule organization and spindle pole body duplication.Semantic proximity Read ↗

New mutations in the core Schizosaccharomyces pombe spindle pole body scaffold Ppc89 reveal separable functions in regulating cell division.Semantic proximity Read ↗

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