Evidence map›Paper›PMID 15635096›Full record

ArticleMolecular biology of the cell2005

J-domain protein CDJ2 and HSP70B are a plastidic chaperone pair that interacts with vesicle-inducing protein in plastids 1.

Cuimin Liu, Felix Willmund, Julian P Whitelegge, Susan Hawat, Bettina Knapp, Mukesh Lodha, Michael Schroda

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

69 citing papers in PubMed, 128 citations in OpenAlex.

  1. VIA1 is a conserved regulator of thylakoid membrane integrity that acts through VIPP1.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Membrane interaction of cyanobacterial and chloroplast ESCRT-III proteins.The Plant journal : for cell and molecular biology · 2026
    Review
  3. Acclimation to high and low diurnal light is flexible inProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
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  13. Developmental acclimation of the thylakoid proteome to light intensity in Arabidopsis.The Plant journal : for cell and molecular biology · 2021
    Article
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  19. ThePlant physiology · 2019
    Article
  20. Article

9 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

7 authors at 2 institutions in 2 countries.

Cuimin LiuPlant Biochemistry, Institute of Biology II, University of Freiburg, D-79104 Freiburg, Germany.
Felix Willmund
Julian P Whitelegge
Susan Hawat
Bettina Knapp
Mukesh Lodha
Michael Schroda
University of Freiburg · DEUniversity of California, Los Angeles · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

J-domain cochaperones confer functional specificity to their heat shock protein (HSP)70 partner by recruiting it to specific substrate proteins. To gain insight into the functions of plastidic HSP70s, we searched in Chlamydomonas databases for expressed sequence tags that potentially encode chloroplast-targeted J-domain cochaperones. Two such cDNAs were found: the encoded J-domain proteins were named chloroplast DnaJ homolog 1 and 2 (CDJ1 and CDJ2). CDJ2 was shown to interact with a approximately 28-kDa protein that by mass spectrometry was identified as the vesicle-inducing protein in plastids 1 (VIPP1). In fractionation experiments, CDJ2 was detected almost exclusively in the stroma, whereas VIPP1 was found in low-density membranes, thylakoids, and in the stroma. Coimmunoprecipitation and mass spectrometry analyses identified stromal HSP70B as the major protein interacting with soluble VIPP1, and, as confirmed by cross-linking data, as chaperone partner of CDJ2. In blue native-PAGE of soluble cell extracts, CDJ2 and VIPP1 comigrated in complexes of >>669, approximately 150, and perhaps approximately 300 kDa. Our data suggest that CDJ2, presumably via coiled-coil interactions, binds to VIPP1 and presents it to HSP70B in the ATP state. Our findings and the previously reported requirement of VIPP1 for the biogenesis of thylakoid membranes point to a role for the HSP70B/CDJ2 chaperone pair in this process.

Indexed as

Adenosine TriphosphateAmino Acid SequenceAnimalsBacterial ProteinsChlamydomonas reinhardtiiCloning, MolecularCross-Linking ReagentsDatabases, GeneticElectrophoresis, Polyacrylamide GelEscherichia coliGlutaralGreen Fluorescent ProteinsHot TemperatureHSP70 Heat-Shock ProteinsImmunoprecipitationLightAdenosine TriphosphateBacterial ProteinsCross-Linking ReagentsGlutaralGreen Fluorescent ProteinsHSP70 Heat-Shock ProteinsHSPA7 protein, humanMacromolecular SubstancesMembrane ProteinsMolecular ChaperonesRNAVIPP1 protein, Synechocystis

Identifiers

PMID15635096
PMCPMC551482
OpenAlexW2168219757

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.