Evidence map›Paper›PMID 20498083›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2010

Regulation of a heterodimeric kinesin-2 through an unprocessive motor domain that is turned processive by its partner.

Melanie Brunnbauer, Felix Mueller-Planitz, Süleyman Kösem, Thi Hieu Ho, Renate Dombi, J Christof M Gebhardt, Matthias Rief, Zeynep Okten

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

48 citing papers in PubMed, 73 citations in OpenAlex.

  1. Article
  2. Regulation of kinesin-2 motility by its β-hairpin motif.Nature structural & molecular biology · 2025
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  3. Article
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  14. Review
  15. The physiological cargo adaptor of kinesin-2 functions as an evolutionary conserved lockpick.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  16. Article
  17. Article
  18. Intraflagellar transport trains and motors: Insights from structure.Seminars in cell & developmental biology · 2020
    Review
  19. Article
  20. The mechanochemistry of the kinesin-2 KIF3AC heterodimer is related to strain-dependent kinetic properties of KIF3A and KIF3C.Proceedings of the National Academy of Sciences of the United States of America · 2020
    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

8 authors at 3 institutions in 1 country.

Melanie BrunnbauerPhysik Department E22, Technische Universität München, James-Franck-Strasse, D-85748 Garching, Germany.
Felix Mueller-Planitz
Süleyman Kösem
Thi Hieu Ho
Renate Dombi
J Christof M Gebhardt
Matthias Rief
Zeynep Okten
Center for Integrated Protein Science Munich · DELudwig-Maximilians-Universität München · DETechnical University of Munich · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cilia are microtubule-based protrusions of the plasma membrane found on most eukaryotic cells. Their assembly is mediated through the conserved intraflagellar transport mechanism. One class of motor proteins involved in intraflagellar transport, kinesin-2, is unique among kinesin motors in that some of its members are composed of two distinct polypeptides. However, the biological reason for heterodimerization has remained elusive. Here we provide several interdependent reasons for the heterodimerization of the kinesin-2 motor KLP11/KLP20 of Caenorhabditis elegans cilia. One motor domain is unprocessive as a homodimer, but heterodimerization with a processive partner generates processivity. The "unprocessive" subunit is kept in this partnership as it mediates an asymmetric autoregulation of the motor activity. Finally, heterodimerization is necessary to bind KAP1, the in vivo link between motor and cargo.

Indexed as

MovementProtein MultimerizationAmino Acid SequenceAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsCiliaKinesinsKineticsMolecular Sequence DataSequence AlignmentCaenorhabditis elegans ProteinsKinesins

Identifiers

PMID20498083
PMCPMC2890855
OpenAlexW2010018522

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.