Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

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

Molecular biology of the cell - 1 Dec 1997

Sundberg H A, Davis T N

Abstract excerpt

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...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Alleles
Share to Binding Sites
Share to Fungal Proteins

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Genes, Fungal

Share to Genetic Complementation Test

Share to Mutation

Share to Nuclear Proteins

Share to Saccharomyces cerevisiae

Source

Open in PubMed Open full text

Identifiers

PMID: 9398677
DOI: 10.1091/mbc.8.12.2575
PMCID: PMC25729

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A mutational analysis identifies three functional regions of the spindle pole component Spc110p in Saccharomyces cerevisiae.PMID 9398677Read ↗

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

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

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

The 110-kD spindle pole body component of Saccharomyces cerevisiae is a phosphoprotein that is modified in a cell cycle-dependent manner.Semantic proximity Read ↗

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

The yeast protein kinase Mps1p is required for assembly of the integral spindle pole body component Spc42p.Semantic proximity Read ↗

Mutational analysis reveals a role for the C terminus of the proteasome subunit Rpt4p in spindle pole body duplication in Saccharomyces cerevisiae.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.