Evidence map›Paper›PMID 16649105›Full record

ArticlePlant molecular biology2006

Identification of a glycosylphosphatidylinositol-anchored plasma membrane protein interacting with the C-terminus of auxin-binding protein 1: a photoaffinity crosslinking study.

Shoji Shimomura

Abstract read
PubMed Publisher
In one paragraph

Article in Plant molecular biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.1field-weighted citation impact, top 12% 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

23 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Article
  3. The Story of Auxin-Binding Protein 1 (ABP1).Cold Spring Harbor perspectives in biology · 2021
    Review
  4. Article
  5. Review
  6. Article
  7. Glycosylphosphatidylinositol-Anchored Proteins inFrontiers in plant science · 2019
    Review
  8. Review
  9. Auxin regulation of cell polarity in plants.Current opinion in plant biology · 2015
    Review
  10. Review
  11. Review
  12. Auxin activity: Past, present, and future.American journal of botany · 2015
    Review
  13. Review
  14. Review
  15. Article
  16. Article
  17. Is ABP1 an auxin receptor yet?Molecular plant · 2011
    Review
  18. Review
  19. Article
  20. 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

1 author at 1 institution in 1 country.

Shoji ShimomuraDepartment of Biochemistry, National Institute of Agrobiological Sciences, Kannondai 2-1-2, Tsukuba, Ibaraki 305-8602, Japan. shimom@affrc.go.jp
Institute of Agrobiological Sciences · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Synthetic peptides corresponding to the C-terminus of auxin-binding protein 1 (ABP1) have been shown to function as auxin agonists. To define a C-terminal receptor, photoaffinity crosslinking experiments were performed using an azido derivative of a C-terminal peptide and plasma membranes from maize (Zea mays L.). The crosslinking reaction was monitored by immunoblotting using anti-ABP1 antibodies. The crosslinked proteins were isolated by 2D gel electrophoresis and identified by mass spectrometric analysis. Further, the noncrosslinked forms of these proteins were also identified. Two proteins with apparent molecular masses of 73 kDa (termed C-terminal peptide-binding protein 1, CBP1) and 35 kDa (CBP2) were specifically linked with the C-terminal peptide. CBP2 is a cytoplasmic protein that consists of two conserved domains that are characteristic of a ricin-type lectin domain. CBP2 remained in the detergent-insoluble particles and was released from the particles by the addition of monosaccharides such as methyl-beta-D-galactopyranoside. CBP1 was released from the membranes by treatment with phosphatidylinositol-specific phospholipase C, indicating that CBP1 is a glycosylphosphatidylinositol (GPI)-anchored plasma membrane protein. CBP1 was found to be a copper-binding protein, and is highly homologous to Arabidopsis thaliana SKU5 that contributes to directional root growth processes. Further, it is similar to A. thaliana SKS6 that contributes to cotyledon vascular patterning and to Nicotiana tabacum NTP303 that contributes to pollen tube growth. The present results indicate that ABP1 may contribute to directional cell growth processes via the GPI-anchored plasma membrane protein SKU5 and its family members.

Indexed as

Amino Acid SequenceCarrier ProteinsCross-Linking ReagentsElectrophoresis, Gel, Two-DimensionalGlycoproteinsGlycosylphosphatidylinositolsImmunoblottingMembrane GlycoproteinsMembrane ProteinsMolecular Sequence DataOligopeptidesPhotoaffinity LabelsPlant ProteinsProtein BindingReceptors, Cell SurfaceSolubilityauxin-binding protein 1Carrier Proteinscolligincopper-binding proteinCross-Linking ReagentsGlycoproteinsGlycosylphosphatidylinositolsMembrane GlycoproteinsMembrane ProteinsOligopeptidesPhotoaffinity LabelsPlant ProteinsReceptors, Cell Surface

Identifiers

PMID16649105
OpenAlexW2049889696

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.