Evidence map›Paper›PMID 16126836›Full record

ArticleThe Plant cell2005

Plasmodesmal-associated protein kinase in tobacco and Arabidopsis recognizes a subset of non-cell-autonomous proteins.

Jung-Youn Lee, Ken-ichiro Taoka, Byung-Chun Yoo, Gili Ben-Nissan, Dong-Jin Kim, William J Lucas

Open access · greenAbstract read
In one paragraph

Article in The Plant cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed, 1 pooled it
14.1field-weighted citation impact, top 1% 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

77 citing papers in PubMed, 1 synthesis or guideline pooled it, 163 citations in OpenAlex.

  1. Pooled it
  2. CabioRxiv : the preprint server for biology · 2026
    Article
  3. Review
  4. Identification ofGenes · 2025
    Article
  5. Silencing of Putative Plasmodesmata-Associated GenesPlants (Basel, Switzerland) · 2025
    Article
  6. Review
  7. Article
  8. Cellular Partners of Tobamoviral Movement Proteins.International journal of molecular sciences · 2025
    Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Article
  20. Article

17 more citing papers are in PubMed but not listed here.

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

6 authors at 3 institutions in 1 country.

Jung-Youn LeeSection of Plant Biology, Division of Biological Sciences, University of California, Davis, CA 95616, USA. lee@dbi.udel.edu
Ken-ichiro Taoka
Byung-Chun Yoo
Gili Ben-Nissan
Dong-Jin Kim
William J Lucas
University of California, Davis · USUniversity of Delaware · USBiotechnology Institute · US

Funding

TOWARDS SOLID-STATE NMR STRUCTURES OF GPCRSP20RR015588 · NCRR · UNIVERSITY OF DELAWARE · PI LENHOFF, ABRAHAM M · 2000 to 2009
$18.2M
NCRR NIH HHS P20 RR015588NCRR NIH HHS P20 RR 15588
6 · The paper itself

Abstract

Cell-to-cell communication in plants involves the trafficking of macromolecules through specialized intercellular organelles, termed plasmodesmata. This exchange of proteins and RNA is likely regulated, and a role for protein phosphorylation has been implicated, but specific components remain to be identified. Here, we describe the molecular characterization of a plasmodesmal-associated protein kinase (PAPK). A 34-kD protein, isolated from a plasmodesmal preparation, exhibits calcium-independent kinase activity and displays substrate specificity in that it recognizes a subset of viral and endogenous non-cell-autonomous proteins. This PAPK specifically phosphorylates the C-terminal residues of tobacco mosaic virus movement protein (TMV MP); this posttranslational modification has been shown to affect MP function. Molecular analysis of purified protein established that tobacco (Nicotiana tabacum) PAPK is a member of the casein kinase I family. Subcellular localization studies identified a possible Arabidopsis thaliana PAPK homolog, PAPK1. TMV MP and PAPK1 are colocalized within cross-walls in a pattern consistent with targeting to plasmodesmata. Moreover, Arabidopsis PAPK1 also phosphorylates TMV MP in vitro at its C terminus. These results strongly suggest that Arabidopsis PAPK1 is a close homolog of tobacco PAPK. Thus, PAPK1 represents a novel plant protein kinase that is targeted to plasmodesmata and may play a regulatory role in macromolecular trafficking between plant cells.

Indexed as

ArabidopsisArabidopsis ProteinsCarrier ProteinsCasein Kinase ICell CommunicationConserved SequenceMolecular Sequence DataNicotianaPhosphorylationPhylogenyPlasmodesmataProtein KinasesProtein Processing, Post-TranslationalProtein TransportSequence Homology, Amino AcidArabidopsis ProteinsCarrier ProteinsCasein Kinase IPAPK1 protein, ArabidopsisProtein Kinases

Identifiers

PMID16126836
PMCPMC1242275
OpenAlexW2114321548

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.