Evidence map›Paper›PMID 8768376›Full record

ArticleThe Plant cell1996

The major integral proteins of spinach leaf plasma membranes are putative aquaporins and are phosphorylated in response to Ca2+ and apoplastic water potential.

I Johansson, C Larsson, B Ek, P Kjellbom

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Plant cell, 1996. 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
5.2field-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

70 citing papers in PubMed, 301 citations in OpenAlex.

  1. Article
  2. Article
  3. Overexpression of theFrontiers in plant science · 2025
    Article
  4. Aquaporin Modulation by Cations, a Review.Current issues in molecular biology · 2024
    Review
  5. Article
  6. Functional Regulation of Aquaporin Dynamics by Lipid Bilayer Composition.bioRxiv : the preprint server for biology · 2023
    Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Review
  12. Salt Stress Signals on Demand: Cellular Events in the Right Context.International journal of molecular sciences · 2020
    Review
  13. Sweet Cherry (International journal of molecular sciences · 2020
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. The Interactions of Aquaporins and Mineral Nutrients in Higher Plants.International journal of molecular sciences · 2016
    Review
  20. Review

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

4 authors at 1 institution in 1 country.

I JohanssonDepartment of Plant Biochemistry, Lund University, Sweden.
C Larsson
B Ek
P Kjellbom
Lund University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We show that homologs of the major intrinsic protein (MIP) family are major integral proteins of the spinach leaf plasma membrane and constitute approximately 20% of integral plasma membrane protein. By using oligonucleotide primers based on partial amino acid sequences for polymerase chain reaction and screening of a spinach leaf cDNA library, we obtained two full-length clones of MIP homologs (pm28a and pm28b). One of these clones, pm28a, was sequenced, and it encodes a protein (PM28A) of 281 amino acids with a molecular mass of 29.9 kD. DNA gel blots indicated that PM28A is the product of a single gene, and RNA gel blots showed that pm28a is ubiquitously expressed in the plant. In vivo phosphorylation of the 28-kD polypeptide(s), corresponding to PM28A and PM28B, was dependent on apoplastic water potential, suggesting a role in regulation of cell turgor for these putative aquaporins. In vitro, only one of the homologs, PM28A, was phosphorylated. Phosphorylation of PM28A occurred on Ser-274, seven amino acids from the C terminus of the protein, within a consensus phosphorylation site (Ser-X-Arg) for vertebrate protein kinase C. In vitro phosphorylation of PM28A was due to a plasma membrane-associated protein kinase and was strictly dependent on submicromolar concentrations of Ca2+.

Indexed as

AquaporinsPlant ProteinsAmino Acid SequenceBase SequenceCalciumCell MembraneCloning, MolecularConsensus SequenceDNA, ComplementaryDNA PrimersGene LibraryMembrane ProteinsModels, StructuralMolecular Sequence DataPhosphorylationPlant LeavesAquaporinsCalciumDNA, ComplementaryDNA PrimersMembrane ProteinsPlant ProteinsPM28A protein, Spinacia oleraceaRecombinant ProteinsWater

Identifiers

PMID8768376
PMCPMC161200
OpenAlexW2148624161

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.