Evidence map›Paper›PMID 15486098›Full record

ArticleThe Plant cell2004

Novel targeting signals mediate the sorting of different isoforms of the tail-anchored membrane protein cytochrome b5 to either endoplasmic reticulum or mitochondria.

Yeen Ting Hwang, Scott M Pelitire, Matthew P A Henderson, David W Andrews, John M Dyer, Robert T Mullen

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

42 citing papers in PubMed, 106 citations in OpenAlex.

  1. A plant-specific cytochromeScience advances · 2025
    Article
  2. Article
  3. Article
  4. Article
  5. CytochromeFrontiers in plant science · 2022
    Review
  6. An endoplasmic reticulum-localized cytochromeProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. CytochromeThe Plant cell · 2019
    Article
  13. Article
  14. Article
  15. Mechanisms of Tail-Anchored Membrane Protein Targeting and Insertion.Annual review of cell and developmental biology · 2017
    Review
  16. Article
  17. Article
  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

6 authors at 4 institutions in 2 countries.

Yeen Ting HwangDepartment of Botany, University of Guelph, Guelph, Ontario N1G 2W1, Canada.
Scott M Pelitire
Matthew P A Henderson
David W Andrews
John M Dyer
Robert T Mullen
McMaster University · CAUniversity of Guelph · CAAgricultural Research Service · USSouthern Regional Research Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Tail-anchored membrane proteins are a class of proteins that are targeted posttranslationally to various organelles and integrated by a single segment of hydrophobic amino acids located near the C terminus. Although the localization of tail-anchored proteins in specific subcellular compartments in plant cells is essential for their biological function, the molecular targeting signals responsible for sorting these proteins are not well defined. Here, we describe the biogenesis of four closely related tung (Aleurites fordii) cytochrome b5 isoforms (Cb5-A, -B, -C, and -D), which are small tail-anchored proteins that play an essential role in many cellular processes, including lipid biosynthesis. Using a combination of in vivo and in vitro assays, we show that Cb5-A, -B, and -C are targeted exclusively to the endoplasmic reticulum (ER), whereas Cb5-D is targeted specifically to mitochondrial outer membranes. Comprehensive mutational analyses of ER and mitochondrial Cb5s revealed that their C termini, including transmembrane domains (TMD) and tail regions, contained several unique physicochemical and sequence-specific characteristics that defined organelle-specific targeting motifs. Mitochondrial targeting of Cb5 was mediated by a combination of hydrophilic amino acids along one face of the TMD, an enrichment of branched beta-carbon-containing residues in the medial portion of the TMD, and a dibasic -R-R/K/H-x motif in the C-terminal tail. By contrast, ER targeting of Cb5 depended primarily upon the overall length and hydrophobicity of the TMD, although an -R/H-x-Y/F- motif in the tail was also a targeting determinant. Collectively, the results presented provide significant insight into the early biogenetic events required for entry of tail-anchored proteins into either the ER or mitochondrial targeting pathways.

Indexed as

AleuritesAmino Acid MotifsAmino Acid SequenceCytochromes b5Endoplasmic ReticulumGene Expression Regulation, PlantIntracellular MembranesMembrane ProteinsMitochondriaMolecular Sequence DataPhylogenyPlant ProteinsProtein IsoformsProtein Sorting SignalsProtein Structure, TertiaryProtein TransportCytochromes b5Membrane ProteinsPlant ProteinsProtein IsoformsProtein Sorting Signals

Identifiers

PMID15486098
PMCPMC527194
OpenAlexW2130926483

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.