Evidence map›Paper›PMID 8106549›Full record

ArticleThe Journal of cell biology1994

Localization of the Kar3 kinesin heavy chain-related protein requires the Cik1 interacting protein.

B D Page, L L Satterwhite, M D Rose, M Snyder

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

68 citing papers in PubMed, 121 citations in OpenAlex.

  1. Article
  2. Kar4, the Yeast Homolog of METTL14, is Required for mRNA mbioRxiv : the preprint server for biology · 2023
    Article
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  19. Article
  20. Kinesin Kar3Cik1 ATPase pathway for microtubule cross-linking.The Journal of biological chemistry · 2011
    Article

8 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

4 authors at 1 institution in 1 country.

B D PageDepartment of Biology, Yale University, New Haven, Connecticut 06520.
L L Satterwhite
M D Rose
M Snyder
Yale University · US

Funding

Mechanisms of Nuclear and Cell Fusion in YeastR01GM037739 · NIGMS · PRINCETON UNIVERSITY · PI ROSE, MARK DAVID · 1987 to 2016
$7.4M
TWO SIGNALING PATHWAYS INVOLVED IN YEAST MORPHOGENESISR01GM036494 · NIGMS · YALE UNIVERSITY · PI SNYDER, MICHAEL P · 1986 to 2007
$2.7M
NIGMS NIH HHS GM36494NIGMS NIH HHS GM37739NIGMS NIH HHS R01 GM037739
6 · The paper itself

Abstract

The Kar3 protein (Kar3p), a protein related to kinesin heavy chain, and the Cik1 protein (Cik1p) appear to participate in the same cellular processes in S. cerevisiae. Phenotypic analysis of mutants indicates that both CIK1 and KAR3 participate in spindle formation and karyogamy. In addition, the expression of both genes is induced by pheromone treatment. In vegetatively growing cells, both Cik1::beta-gal and Kar3::beta-gal fusions localize to the spindle pole body (SPB), and after pheromone treatment both fusion proteins localize to the spindle pole body and cytoplasmic microtubules. The dependence of Cik1p and Kar3p localization upon one another was investigated by indirect immunofluorescence of fusion proteins in pheromone-treated cells. The Cik1p::beta-gal fusion does not localize to the SPB or microtubules in a kar3 delta strain, and the Kar3p::beta-gal fusion protein does not localize to microtubule-associated structures in a cik1 delta strain. Thus, these proteins appear to be interdependent for localization to the SPB and microtubules. Analysis by both the two-hybrid system and co-immunoprecipitation experiments indicates that Cik1p and kar3p interact, suggesting that they are part of the same protein complex. These data indicate that interaction between a putative kinesin heavy chain-related protein and another protein can determine the localization of motor activity and thereby affect the functional specificity of the motor complex.

Indexed as

Microtubule-Associated ProteinsMicrotubule ProteinsSaccharomyces cerevisiae ProteinsCytoplasmFluorescent Antibody TechniqueFungal ProteinsImmunohistochemistryKaryotypingMicrotubulesPhenotypePheromonesPrecipitin TestsSaccharomyces cerevisiaeCIK1 protein, S cerevisiaeFungal ProteinsKAR3 protein, S cerevisiaeMicrotubule-Associated ProteinsMicrotubule ProteinsPheromonesSaccharomyces cerevisiae Proteins

Identifiers

PMID8106549
PMCPMC2119913
OpenAlexW2123527149

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.