Evidence map›Paper›PMID 18065692›Full record

ArticleThe Plant cell2007

Two distinct forms of M-locus protein kinase localize to the plasma membrane and interact directly with S-locus receptor kinase to transduce self-incompatibility signaling in Brassica rapa.

Mitsuru Kakita, Kohji Murase, Megumi Iwano, Tomohito Matsumoto, Masao Watanabe, Hiroshi Shiba, Akira Isogai, Seiji Takayama

Open access · greenAbstract read
In one paragraph

Article in The Plant cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

70 citing papers in PubMed, 175 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Review
  5. Characterization of self-incompatibility genes inFrontiers in plant science · 2026
    Article
  6. Article
  7. Article
  8. Peptides in plant reproduction-small yet powerful.Frontiers in plant science · 2025
    Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Molecular mechanisms of self-incompatibility in Brassicaceae and Solanaceae.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2024
    Review
  15. Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. Article

10 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

8 authors at 2 institutions in 1 country.

Mitsuru KakitaGraduate School of Biological Sciences, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma 630-0192, Japan.
Kohji Murase
Megumi Iwano
Tomohito Matsumoto
Masao Watanabe
Hiroshi Shiba
Akira Isogai
Seiji Takayama
Nara Institute of Science and Technology · JPTohoku University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many flowering plants possess systems of self-incompatibility (SI) to prevent inbreeding. In Brassica, SI recognition is controlled by the multiallelic gene complex (S-haplotypes) at the S-locus, which encodes both the male determinant S-locus protein 11 (SP11/SCR) and the female determinant S-receptor kinase (SRK). Upon self-pollination, the S-haplotype-specific interaction between the pollen-borne SP11 and the cognate stigmatic SRK receptor induces SI signaling in the stigmatic papilla cell and results in rejection of the self-pollen. Our genetic analysis of a self-compatible mutant revealed the involvement of a cytoplasmic protein kinase, M-locus protein kinase (MLPK), in the SI signaling, but its exact physiological function remains unknown. In this study, we identified two different MLPK transcripts, MLPKf1 and MLPKf2, which are produced using alternative transcriptional initiation sites and encode two isoforms that differ only at the N termini. While MLPKf1 and MLPKf2 exhibited distinct expression profiles, both were expressed in papilla cells. MLPKf1 localizes to the plasma membrane through its N-terminal myristoylation motif, while MLPKf2 localizes to the plasma membrane through its N-terminal hydrophobic region. Although both MLPKf1 and MLPKf2 could independently complement the mlpk/mlpk mutation, their mutant forms that lack the plasma membrane localization motifs failed to complement the mutation. Furthermore, a bimolecular fluorescence complementation assay revealed direct interactions between SRK and the MLPK isoforms in planta. These results suggest that MLPK isoforms localize to the papilla cell membrane and interact directly with SRK to transduce SI signaling.

Indexed as

Alternative SplicingAmino Acid SequenceBase SequenceBrassica rapaCell MembraneGene Expression Regulation, PlantGenetic Complementation TestIn Situ HybridizationMolecular Sequence DataMutationPlant ProteinsPlants, Genetically ModifiedProtein BindingProtein IsoformsProtein KinasesReverse Transcriptase Polymerase Chain ReactionPlant ProteinsProtein IsoformsProtein Kinases

Identifiers

PMID18065692
PMCPMC2217645
OpenAlexW2135503930

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.