Evidence map›Paper›PMID 24930965›Full record

ArticleCurrent biology : CB2014

Assembling the protein architecture of the budding yeast kinetochore-microtubule attachment using FRET.

Pavithra Aravamudhan, Isabella Felzer-Kim, Kaushik Gurunathan, Ajit P Joglekar

Open access · bronzeAbstract read
In one paragraph

Article in Current biology : CB, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
3.8field-weighted citation impact, top 7% 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

46 citing papers in PubMed, 68 citations in OpenAlex.

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  16. Investigating eukaryotic cells with cryo-ET.Molecular biology of the cell · 2020
    Article
  17. FRET Microscopy in Yeast.Biosensors · 2019
    Review
  18. Article
  19. Article
  20. Article
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 2 institutions in 2 countries.

Pavithra AravamudhanBiophysics, University of Michigan, 930 North University Avenue, Ann Arbor, MI 48109-1055, USA.
Isabella Felzer-KimCell and Developmental Biology, University of Michigan, 109 Zina Pitcher Place, Ann Arbor, MI 48109, USA.
Kaushik GurunathanSastra University, Tirumalaisamudram, Thanjavur, Tamil Nadu 613402, India.
Ajit P JoglekarBiophysics, University of Michigan, 930 North University Avenue, Ann Arbor, MI 48109-1055, USA; Cell and Developmental Biology, University of Michigan, 109 Zina Pitcher Place, Ann Arbor, MI 48109, USA. Electronic address: ajitj@umich.edu.
University of Michigan–Ann Arbor · USSASTRA University · IN

Funding

Architecture-function analysis of the kinetochore motorR01GM105948 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI JOGLEKAR, AJIT · 2013 to 2017
$1.4M
NIGMS NIH HHS R01 GM105948NIGMS NIH HHS R01-GM-105948Wellcome Trust
6 · The paper itself

Abstract

backgroundThe kinetochore is a multiprotein machine that couples chromosome movement to microtubule (MT) polymerization and depolymerization. It uses numerous copies of at least three MT-binding proteins to generate bidirectional movement. The nanoscale organization of these proteins within the kinetochore plays an important role in shaping the mechanisms that drive persistent, bidirectional movement of the kinetochore.

resultsWe used fluorescence resonance energy transfer (FRET) between genetically encoded fluorescent proteins fused to kinetochore subunits to reconstruct the nanoscale organization of the budding yeast kinetochore. We performed >60 FRET and high-resolution colocalization measurements involving the essential MT-binding kinetochore components: Ndc80, Dam1, Spc105, and Stu2. These measurements reveal that neighboring Ndc80 complexes within the kinetochore are narrowly distributed along the length of the MT. Dam1 complex molecules are concentrated near the MT-binding domains of Ndc80. Stu2 localizes in high abundance within a narrowly defined territory within the kinetochore centered ∼20 nm on the centromeric side of the Dam1 complex.

conclusionsOur data show that the MT attachment site of the budding yeast kinetochore is well organized. Ndc80, Dam1, and Stu2 are all narrowly distributed about their average positions along the kinetochore-MT axis. The relative organization of these components, their narrow distributions, and their known MT-binding properties together elucidate how their combined actions generate persistent, bidirectional kinetochore movement coupled to MT polymerization and depolymerization.

Indexed as

Models, BiologicalCell Cycle ProteinsFluorescence Resonance Energy TransferKinetochoresMicrotubule-Associated ProteinsMicrotubulesMultiprotein ComplexesNuclear ProteinsSaccharomyces cerevisiae ProteinsSaccharomycetalesCell Cycle ProteinsDAM1 protein, S cerevisiaeMicrotubule-Associated ProteinsMultiprotein ComplexesNDC80 protein, S cerevisiaeNuclear ProteinsSaccharomyces cerevisiae ProteinsSTU2 protein, S cerevisiae

Identifiers

PMID24930965
PMCPMC4320969
OpenAlexW2028604863

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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.