Evidence map›Paper›PMID 29540705›Full record

ArticleNature communications2018

The preprophase band-associated kinesin-14 OsKCH2 is a processive minus-end-directed microtubule motor.

Kuo-Fu Tseng, Pan Wang, Yuh-Ru Julie Lee, Joel Bowen, Allison M Gicking, Lijun Guo, Bo Liu, Weihong Qiu

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

17 citing papers in PubMed, 33 citations in OpenAlex.

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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

8 authors at 3 institutions in 2 countries.

Kuo-Fu TsengDepartment of Physics, Oregon State University, Corvallis, OR, 97331, USA.
Pan WangDepartment of Physics, Oregon State University, Corvallis, OR, 97331, USA.
Yuh-Ru Julie LeeDepartment of Plant Biology, University of California at Davis, Davis, CA, 95616, USA.
Joel BowenDepartment of Mathematics, Oregon State University, Corvallis, OR, 97331, USA.
Allison M GickingDepartment of Physics, Oregon State University, Corvallis, OR, 97331, USA.
Lijun GuoInstitute of Photobiophysics, Henan University, Kaifeng, 475004, Henan, China.
Bo LiuDepartment of Plant Biology, University of California at Davis, Davis, CA, 95616, USA. BLiu@ucdavis.edu.ORCID http://orcid.org/0000-0002-6234-7451
Weihong QiuDepartment of Physics, Oregon State University, Corvallis, OR, 97331, USA. Weihong.Qiu@physics.oregonstate.edu.ORCID http://orcid.org/0000-0003-1413-1389
Oregon State University · USHenan University · CNUniversity of California, Davis · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In animals and fungi, cytoplasmic dynein is a processive minus-end-directed motor that plays dominant roles in various intracellular processes. In contrast, land plants lack cytoplasmic dynein but contain many minus-end-directed kinesin-14s. No plant kinesin-14 is known to produce processive motility as a homodimer. OsKCH2 is a plant-specific kinesin-14 with an N-terminal actin-binding domain and a central motor domain flanked by two predicted coiled-coils (CC1 and CC2). Here, we show that OsKCH2 specifically decorates preprophase band microtubules in vivo and transports actin filaments along microtubules in vitro. Importantly, OsKCH2 exhibits processive minus-end-directed motility on single microtubules as individual homodimers. We find that CC1, but not CC2, forms the coiled-coil to enable OsKCH2 dimerization. Instead, our results reveal that removing CC2 renders OsKCH2 a nonprocessive motor. Collectively, these results show that land plants have evolved unconventional kinesin-14 homodimers with inherent minus-end-directed processivity that may function to compensate for the loss of cytoplasmic dynein.

Indexed as

AnimalsBiological TransportCytoplasmCytoskeletonDyneinsKinesinsMicrotubulesMolecular Motor ProteinsProtein BindingDyneinsKinesinsMolecular Motor Proteins

Identifiers

PMID29540705
PMCPMC5852081
OpenAlexW2951558448

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.