Evidence map›Paper›PMID 9247651›Full record

ArticleMolecular biology of the cell1997

Aip3p/Bud6p, a yeast actin-interacting protein that is involved in morphogenesis and the selection of bipolar budding sites.

D C Amberg, J E Zahner, J W Mulholland, J R Pringle, D Botstein

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers.

0numbers the graph read from it
0cells of the map it votes in
86citing papers in PubMed
5.0field-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

86 citing papers in PubMed, 170 citations in OpenAlex.

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  14. Review
  15. Deconstructing formin-dependent actin cable assembly.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  16. Article
  17. Article
  18. Structure of the formin-interaction domain of the actin nucleation-promoting factor Bud6.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  19. Article
  20. Review

26 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

5 authors at 1 institution in 1 country.

D C AmbergDepartment of Genetics, Stanford University School of Medicine, California 94305-5120, USA.
J E Zahner
J W Mulholland
J R Pringle
D Botstein
Stanford University · US

Funding

Genetics of Functional Interactions in YeastR01GM046406 · NIGMS · STANFORD UNIVERSITY · PI BOTSTEIN, DAVID · 2001 to 2015
$9.5M
MORPHOGENESIS AND CYTOKINESIS IN THE YEAST CELL CYCLER37GM031006 · NIGMS · UNIVERSITY OF NORTH CAROLINA CHAPEL HILL · PI PRINGLE, JOHN R · 2000 to 2010
$4.8M
GENETICS OF FUNCTIONAL INTERACTIONS IN YEASTR37GM046406 · NIGMS · STANFORD UNIVERSITY · PI BOTSTEIN, DAVID · 1991 to 2000
$683k
GENETIC STUDY OF THE YEAST CELL CYCLER01GM031006 · NIGMS · UNIVERSITY OF NORTH CAROLINA CHAPEL HILL · PI PRINGLE, JOHN R · 1986 to 1999
–
PROTEIN STRUCTURE/FUNCTION STUDY IN LIVING CELLR01GM046888 · NIGMS · STANFORD UNIVERSITY · PI BOTSTEIN, DAVID · 1992 to 1995
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NIGMS NIH HHS GM-31006NIGMS NIH HHS GM-46406NIGMS NIH HHS GM-46888
6 · The paper itself

Abstract

A search for Saccharomyces cerevisiae proteins that interact with actin in the two-hybrid system and a screen for mutants that affect the bipolar budding pattern identified the same gene, AIP3/BUD6. This gene is not essential for mitotic growth but is necessary for normal morphogenesis. MATa/alpha daughter cells lacking Aip3p place their first buds normally at their distal poles but choose random sites for budding in subsequent cell cycles. This suggests that actin and associated proteins are involved in placing the bipolar positional marker at the division site but not at the distal tip of the daughter cell. In addition, although aip3 mutant cells are not obviously defective in the initial polarization of the cytoskeleton at the time of bud emergence, they appear to lose cytoskeletal polarity as the bud enlarges, resulting in the formation of cells that are larger and rounder than normal. aip3 mutant cells also show inefficient nuclear migration and nuclear division, defects in the organization of the secretory system, and abnormal septation, all defects that presumably reflect the involvement of Aip3p in the organization and/or function of the actin cytoskeleton. The sequence of Aip3p is novel but contains a predicted coiled-coil domain near its C terminus that may mediate the observed homo-oligomerization of the protein. Aip3p shows a distinctive localization pattern that correlates well with its likely sites of action: it appears at the presumptive bud site prior to bud emergence, remains near the tips of small bund, and forms a ring (or pair of rings) in the mother-bud neck that is detectable early in the cell cycle but becomes more prominent prior to cytokinesis. Surprisingly, the localization of Aip3p does not appear to require either polarized actin or the septin proteins of the neck filaments.

Indexed as

Saccharomyces cerevisiae ProteinsActinsCloning, MolecularFungal ProteinsGene DeletionMicrofilament ProteinsMolecular Sequence DataMutationRecombinant Fusion ProteinsSaccharomyces cerevisiaeSelection, GeneticSequence AnalysisActinsBUD6 protein, S cerevisiaeFungal ProteinsMicrofilament ProteinsRecombinant Fusion ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID9247651
PMCPMC276122
OpenAlexW2086779162

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.