Evidence map›Paper›PMID 10749926›Full record

ArticleMolecular biology of the cell2000

A mutation in gamma-tubulin alters microtubule dynamics and organization and is synthetically lethal with the kinesin-like protein pkl1p.

J L Paluh, E Nogales, B R Oakley, K McDonald, A L Pidoux, W Z Cande

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
4.3field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

62 citing papers in PubMed, 121 citations in OpenAlex.

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2 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 2 countries.

J L PaluhDepartment of Molecular Biology, University of California, Berkeley, California 94720-3200, USA. jlpaluh@socrates.berkeley.edu
E Nogales
B R Oakley
K McDonald
A L Pidoux
W Z Cande
University of California, Berkeley · USThe Ohio State University · USWestern General Hospital · GB

Funding

TUBULIN STRUCTURE BY ELECTRON CRYSTALLOGRAPHYP01GM051487 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI NOGALES, EVA · 1994 to 2018
$27.6M
THE MOLECULAR BIOLOGY OF ORGNELLAR TRANSLOCATIONR01GM031837 · NIGMS · UNIVERSITY OF KANSAS LAWRENCE · PI OAKLEY, BERL RAY · 1985 to 2009
$2.9M
CYTOLOGY/GENETICS OF CHROMOSOME MOVEMENT IN S POMBEF32GM019145 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI PALUH, JANET L · 1997 to 1999
–
FUNCTIONAL MODEL FOR MITOSIS IN CELL LINESR01GM023238 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI CANDE, W ZACHEUS · 1985 to 1999
–
NIGMS NIH HHS 5 F32 GM-19145-02NIGMS NIH HHS F32 GM019145NIGMS NIH HHS GM-23238NIGMS NIH HHS GM-51487NIGMS NIH HHS P01 GM051487NIGMS NIH HHS R01 GM031837
6 · The paper itself

Abstract

Mitotic segregation of chromosomes requires spindle pole functions for microtubule nucleation, minus end organization, and regulation of dynamics. gamma-Tubulin is essential for nucleation, and we now extend its role to these latter processes. We have characterized a mutation in gamma-tubulin that results in cold-sensitive mitotic arrest with an elongated bipolar spindle but impaired anaphase A. At 30 degrees C cytoplasmic microtubule arrays are abnormal and bundle into single larger arrays. Three-dimensional time-lapse video microscopy reveals that microtubule dynamics are altered. Localization of the mutant gamma-tubulin is like the wild-type protein. Prediction of gamma-tubulin structure indicates that non-alpha/beta-tubulin protein-protein interactions could be affected. The kinesin-like protein (klp) Pkl1p localizes to the spindle poles and spindle and is essential for viability of the gamma-tubulin mutant and in multicopy for normal cell morphology at 30 degrees C. Localization and function of Pkl1p in the mutant appear unaltered, consistent with a redundant function for this protein in wild type. Our data indicate a broader role for gamma-tubulin at spindle poles in regulating aspects of microtubule dynamics and organization. We propose that Pkl1p rescues an impaired function of gamma-tubulin that involves non-tubulin protein-protein interactions, presumably with a second motor, MAP, or MTOC component.

Indexed as

Schizosaccharomyces pombe ProteinsAmino Acid SequenceChromosome SegregationFluorescent Antibody TechniqueFungal ProteinsKinesinsMicroscopy, ElectronMicroscopy, VideoMicrotubulesModels, MolecularMolecular Sequence DataMutationProtein Structure, TertiarySchizosaccharomycesSequence AlignmentTubulinFungal ProteinsKinesinsPKL1 protein, S pombeSchizosaccharomyces pombe ProteinsTubulin

Identifiers

PMID10749926
PMCPMC14843
OpenAlexW2107229020

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.