Evidence map›Paper›PMID 18431466›Full record

ArticlePloS one2008

SAM domain-based protein oligomerization observed by live-cell fluorescence fluctuation spectroscopy.

Brian D Slaughter, Joseph M Huff, Winfried Wiegraebe, Joel W Schwartz, Rong Li

Abstract read
In one paragraph

Article in PloS one, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
–field-weighted citation impact
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

24 citing papers in PubMed.

  1. Characterization of anPathogens (Basel, Switzerland) · 2023
    Article
  2. The Adaptor Protein UvSte50 Governs Fungal Pathogenicity ofJournal of fungi (Basel, Switzerland) · 2022
    Article
  3. Article
  4. Loss of a highly conserved sterile alpha motif domain gene (Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
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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.

Brian D SlaughterThe Stowers Institute for Medical Research, Kansas City, Missouri, United States of America.
Joseph M Huff
Winfried Wiegraebe
Joel W Schwartz
Rong Li

Funding

Mechanisms of cell polarization in yeastR01GM057063 · NIGMS · STOWERS INSTITUTE FOR MEDICAL RESEARCH · PI LI, RONG · 1998 to 2015
$5.3M
Advanced imaging tools to examine interactions, dynamics of secretory componenetsF32GM077923 · NIGMS · STOWERS INSTITUTE FOR MEDICAL RESEARCH · PI SLAUGHTER, BRIAN · 2007 to 2008
$96k
NIGMS NIH HHS F32 GM077923NIGMS NIH HHS F32 GM077923-01A1NIGMS NIH HHS GM057063NIGMS NIH HHS R01 GM057063
6 · The paper itself

Abstract

Sterile-alpha-motif (SAM) domains are common protein interaction motifs observed in organisms as diverse as yeast and human. They play a role in protein homo- and hetero-interactions in processes ranging from signal transduction to RNA binding. In addition, mutations in SAM domain and SAM-mediated oligomers have been linked to several diseases. To date, the observation of heterogeneous SAM-mediated oligomers in vivo has been elusive, which represents a common challenge in dissecting cellular biochemistry in live-cell systems. In this study, we report the oligomerization and binding stoichiometry of high-order, multi-component complexes of (SAM) domain proteins Ste11 and Ste50 in live yeast cells using fluorescence fluctuation methods. Fluorescence cross-correlation spectroscopy (FCCS) and 1-dimensional photon counting histogram (1dPCH) confirm the SAM-mediated interaction and oligomerization of Ste11 and Ste50. Two-dimensional PCH (2dPCH), with endogenously expressed proteins tagged with GFP or mCherry, uniquely indicates that Ste11 and Ste50 form a heterogeneous complex in the yeast cytosol comprised of a dimer of Ste11 and a monomer of Ste50. In addition, Ste50 also exists as a high order oligomer that does not interact with Ste11, and the size of this oligomer decreases in response to signals that activate the MAP kinase cascade. Surprisingly, a SAM domain mutant of Ste50 disrupted not only the Ste50 oligomers but also Ste11 dimerization. These results establish an in vivo model of Ste50 and Ste11 homo- and hetero-oligomerization and highlight the usefulness of 2dPCH for quantitative dissection of complex molecular interactions in genetic model organisms such as yeast.

Indexed as

Microbial ViabilityDiffusionGreen Fluorescent ProteinsMAP Kinase Kinase KinasesPhotonsProtein BindingProtein Structure, QuaternaryProtein Structure, TertiaryRecombinant Fusion ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSpectrometry, FluorescenceGreen Fluorescent ProteinsMAP Kinase Kinase KinasesRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsSte11 protein, S cerevisiaeSTE50 protein, S cerevisiae

Identifiers

PMID18431466
PMCPMC2291563

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LicenceCC BY
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Registered trials

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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.