Evidence map›Paper›PMID 29122988›Full record

ArticlePlant physiology2018

KinG Is a Plant-Specific Kinesin That Regulates Both Intra- and Intercellular Movement of SHORT-ROOT.

Ziv Spiegelman, Chin-Mei Lee, Kimberly L Gallagher

Open access · hybridAbstract read
In one paragraph

Article in Plant physiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
7.6field-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

19 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Review
  3. Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Review
  5. Review
  6. Article
  7. Review
  8. Asymmetric cell division in plant development.Journal of integrative plant biology · 2023
    Review
  9. Review
  10. Article
  11. Review
  12. Intercellular trafficking via plasmodesmata: molecular layers of complexity.Cellular and molecular life sciences : CMLS · 2021
    Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. 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

3 authors at 1 institution in 1 country.

Ziv SpiegelmanDepartment of Biology, University of Pennsylvania, Philadelphia, Pennsylvania 19104.ORCID 0000-0003-4876-5072
Chin-Mei LeeDepartment of Biology, University of Pennsylvania, Philadelphia, Pennsylvania 19104.ORCID 0000-0003-3870-4268
Kimberly L GallagherDepartment of Biology, University of Pennsylvania, Philadelphia, Pennsylvania 19104 gallagkl@sas.upenn.edu.ORCID 0000-0002-4942-8855
University of Pennsylvania · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Both endogenous plant proteins and viral movement proteins associate with microtubules to promote their movement through plasmodesmata. The association of viral movement proteins with microtubules facilitates the formation of virus-associated replication complexes, which are required for the amplification and subsequent spread of the virus. However, the role of microtubules in the intercellular movement of plant proteins is less clear. Here we show that the SHORT-ROOT (SHR) protein, which moves between cells in the root to regulate root radial patterning, interacts with a type-14 kinesin, KINESIN G (KinG). KinG is a calponin homology domain kinesin that directly interacts with the SHR-binding protein SIEL (SHR-INTERACING EMBRYONIC LETHAL) and localizes to both microtubules and actin. Since SIEL and SHR associate with endosomes, we suggest that KinG serves as a linker between SIEL, SHR, and the plant cytoskeleton. Loss of KinG function results in a decrease in the intercellular movement of SHR and an increase in the sensitivity of SHR movement to treatment with oryzalin. Examination of SHR and KinG localization and dynamics in live cells suggests that KinG is a nonmotile kinesin that promotes the pausing of SHR-associated endosomes. We suggest a model in which interaction of KinG with SHR allows for the formation of stable movement complexes that facilitate the cell-to-cell transport of SHR.

Indexed as

ActinsArabidopsisArabidopsis ProteinsBridged Bicyclo Compounds, HeterocyclicDinitrobenzenesEndosomesExtracellular SpaceIntracellular SpaceKinesinsMeristemMicrotubulesModels, BiologicalMutationNicotianaPlant EpidermisPlant LeavesActinsArabidopsis ProteinsBridged Bicyclo Compounds, HeterocyclicDinitrobenzenesKinesinsKinG protein, Arabidopsislatrunculin BoryzalinSHORT ROOT protein, ArabidopsisSulfanilamidesThiazolidinesTranscription Factors

Identifiers

PMID29122988
PMCPMC5761801
OpenAlexW2767866206

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.