Evidence map›Paper›PMID 25203210›Full record

ArticleDevelopmental cell2014

An ankyrin repeat domain of AKR2 drives chloroplast targeting through coincident binding of two chloroplast lipids.

Dae Heon Kim, Mi-Jeong Park, Gwang Hyeon Gwon, Antonina Silkov, Zheng-Yi Xu, Eun Chan Yang, Seohyeon Song, Kyungyoung Song, Younghyun Kim, Hwan Su Yoon and 4 more

Open access · bronzeAbstract read
In one paragraph

Article in Developmental cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

25 citing papers in PubMed, 55 citations in OpenAlex.

  1. Cellular Partners of Tobamoviral Movement Proteins.International journal of molecular sciences · 2025
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  12. Genome wide association mapping of epi-cuticular wax genes inPhysiology and molecular biology of plants : an international journal of functional plant biology · 2020
    Article
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  16. Review
  17. Article
  18. Review
  19. Review
  20. TRPA1 ankyrin repeat six interacts with a small molecule inhibitor chemotype.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

14 authors at 4 institutions in 2 countries.

Dae Heon KimDivision of Molecular and Life Sciences, Pohang University of Science and Technology, Pohang 790-784, Korea.
Mi-Jeong ParkDivision of Integrative Biosciences and Biotechnology, Pohang University of Science and Technology, Pohang 790-784, Korea.
Gwang Hyeon GwonDivision of Molecular and Life Sciences, Pohang University of Science and Technology, Pohang 790-784, Korea.
Antonina SilkovDepartment of Biochemistry and Molecular Biophysics, Howard Hughes Medical Institute, Columbia University, New York, NY 11032, USA.
Zheng-Yi XuDivision of Molecular and Life Sciences, Pohang University of Science and Technology, Pohang 790-784, Korea.
Eun Chan YangDepartment of Biological Sciences, Sungkyunkwan University, Suwon 440-746, Korea.
Seohyeon SongDepartment of Chemistry, University of Illinois at Chicago, Chicago, IL 60607, USA.
Kyungyoung SongDivision of Molecular and Life Sciences, Pohang University of Science and Technology, Pohang 790-784, Korea.
Younghyun KimDivision of Molecular and Life Sciences, Pohang University of Science and Technology, Pohang 790-784, Korea.
Hwan Su YoonDepartment of Biological Sciences, Sungkyunkwan University, Suwon 440-746, Korea.
Barry HonigDepartment of Biochemistry and Molecular Biophysics, Howard Hughes Medical Institute, Columbia University, New York, NY 11032, USA.
Wonhwa ChoDivision of Integrative Biosciences and Biotechnology, Pohang University of Science and Technology, Pohang 790-784, Korea; Department of Chemistry, University of Illinois at Chicago, Chicago, IL 60607, USA. Electronic address: wcho@uic.edu.
Yunje ChoDivision of Molecular and Life Sciences, Pohang University of Science and Technology, Pohang 790-784, Korea. Electronic address: yunje@postech.ac.kr.
Inhwan HwangDivision of Molecular and Life Sciences, Pohang University of Science and Technology, Pohang 790-784, Korea; Division of Integrative Biosciences and Biotechnology, Pohang University of Science and Technology, Pohang 790-784, Korea. Electronic address: ihhwang@postech.ac.kr.
Pohang University of Science and Technology · KRHoward Hughes Medical Institute · USSungkyunkwan University · KRUniversity of Illinois Chicago · US

Funding

University of Georgia ProjectU54GM094597 · NIGMS · RUTGERS, THE STATE UNIV OF N.J. · PI MONTELIONE, GAETANO T · 2010 to 2014
$36.9M
COMPUTER STUDIES OF PROTEIN STRUCTURE AND FUNCTIONR01GM030518 · NIGMS · COLUMBIA UNIV NEW YORK MORNINGSIDE · PI HONIG, BARRY H · 1985 to 2020
$4.5M
Membrane Targeting by Phosphoinositide-Binding ProteinsR01GM068849 · NIGMS · UNIVERSITY OF ILLINOIS AT CHICAGO · PI CHO, WONHWA · 2003 to 2015
$3.9M
COMPUTER STUDIES OF PROTEIN STRUCTURE AND FUNCTIONR37GM030518 · NIGMS · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI HONIG, BARRY H · 1995 to 2004
$1.5M
Regulatory Roles of Cellular CholesterolR01GM110128 · NIGMS · UNIVERSITY OF ILLINOIS AT CHICAGO · PI CHO, WONHWA · 2014 to 2016
$1.2M
NIGMS NIH HHS GM30518NIGMS NIH HHS GM68849NIGMS NIH HHS R01 GM030518NIGMS NIH HHS R01 GM068849NIGMS NIH HHS R01 GM110128NIGMS NIH HHS R37 GM030518NIGMS NIH HHS U54 GM094597
6 · The paper itself

Abstract

In organellogenesis of the chloroplast from endosymbiotic cyanobacteria, the establishment of protein-targeting mechanisms to the chloroplast should have been pivotal. However, it is still mysterious how these mechanisms were established and how they work in plant cells. Here we show that AKR2A, the cytosolic targeting factor for chloroplast outer membrane (COM) proteins, evolved from the ankyrin repeat domain (ARD) of the host cell by stepwise extensions of its N-terminal domain and that two lipids, monogalactosyldiacylglycerol (MGDG) and phosphatidylglycerol (PG), of the endosymbiont were selected to function as the AKR2A receptor. Structural analysis, molecular modeling, and mutational analysis of the ARD identified two adjacent sites for coincidental and synergistic binding of MGDG and PG. Based on these findings, we propose that the targeting mechanism of COM proteins was established using components from both the endosymbiont and host cell through a modification of the protein-protein-interacting ARD into a lipid binding domain.

Indexed as

Ankyrin RepeatAmino Acid SequenceArabidopsisArabidopsis ProteinsBinding SitesChloroplastsCyanobacteriaCytosolGalactolipidsLipidsModels, MolecularMolecular ChaperonesMolecular Sequence DataPhosphatidylglycerolsProtein BindingProtein Structure, TertiaryAKR2 protein, ArabidopsisArabidopsis ProteinsGalactolipidsLipidsMolecular ChaperonesmonogalactosyldiacylglycerolPhosphatidylglycerols

Identifiers

PMID25203210
PMCPMC4170656
OpenAlexW2158612448

What OpenQuestion holds

Textmetadata
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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.