Evidence map›Paper›PMID 18477614›Full record

ArticleJournal of cell science2008

Identification of a novel N-terminal hydrophobic sequence that targets proteins to lipid droplets.

John K Zehmer, René Bartz, Pingsheng Liu, Richard G W Anderson

Open access · bronzeAbstract read
In one paragraph

Article in Journal of cell science, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
4.2field-weighted citation impact, top 6% 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

76 citing papers in PubMed, 114 citations in OpenAlex.

  1. Review
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  5. Review
  6. Expression pattern, subcellular localization ofApplied and environmental microbiology · 2025
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  14. METTL7A (TMT1A) and METTL7B (TMT1B) Are Responsible for AlkylDrug metabolism and disposition: the biological fate of chemicals · 2023
    Article
  15. A Novel Localization of METTL7A in Bergmann Glial Cells in Human Cerebellum.International journal of molecular sciences · 2023
    Article
  16. Article
  17. Article
  18. Recent progress in strategies for steroid production in yeasts.World journal of microbiology & biotechnology · 2022
    Review
  19. Article
  20. Induction of mJournal of experimental & clinical cancer research : CR · 2022
    Article

16 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.

John K ZehmerDepartment of Cell Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390-9039, USA.
René Bartz
Pingsheng Liu
Richard G W Anderson
The University of Texas Southwestern Medical Center · US

Funding

TRANSCRIPTIONAL REGULATION OF LDL RECEPTOR PROMOTERP01HL020948 · NHLBI · UT SOUTHWESTERN MEDICAL CENTER · PI GOLDSTEIN, JOSEPH L · 1985 to 2021
$103.1M
FUNCTION OF CAVEOLAE IN POTOCYTOSIS AND CELL SIGNALINGR01GM052016 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI MICHAELY, PETER A. · 1995 to 2010
$4.9M
Regulation of caveolae internalizationF32GM070117 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI ZEHMER, JOHN K · 2004 to 2006
$134k
NHLBI NIH HHS HL 20948NHLBI NIH HHS P01 HL020948NIGMS NIH HHS F32 GM070117NIGMS NIH HHS GM 52016NIGMS NIH HHS GM 70117NIGMS NIH HHS R01 GM052016
6 · The paper itself

Abstract

AAM-B is a putative methyltransferase that is a resident protein of lipid droplets. We have identified an N-terminal 28 amino acid hydrophobic sequence that is necessary and sufficient for targeting the protein to droplets. This sequence will also insert AAM-B into the endoplasmic reticulum (ER). A similar hydrophobic sequence (1-23) in the cytochrome p450 2C9 cannot substitute for 1-28 and only inserts AAM-B into the ER, which indicates that hydrophobicity and ER anchoring are not sufficient to reach the droplet. We found that a similar N-terminal hydrophobic sequence in cytochrome b5 reductase 3 and ALDI could also heterologously target proteins to droplets. Targeting is not affected by changing a conserved proline residue that potentially facilitates the formation of a hairpin loop to leucine. By contrast, targeting is blocked when AAM-B amino acids 59-64 or 65-70, situated downstream of the hydrophobic sequence, are changed to alanines. AAM-B-GFP expressed in Saccharomyces cerevisiae is also faithfully targeted to lipid bodies, indicating that the targeting mechanism is evolutionarily conserved. In conclusion, a class of hydrophobic sequences exists that when placed at the N-terminus of a protein will cause it to accumulate in droplets and in the ER.

Indexed as

Amino Acid SequenceAmino Acid SubstitutionAnimalsChlorocebus aethiopsCOS CellsCytoplasmEndoplasmic ReticulumHeLa CellsHumansHydrophobic and Hydrophilic InteractionsInclusion BodiesIntracellular MembranesLipid MetabolismLipidsMembrane ProteinsMethyltransferasesAAM-B protein, humanLipidsMembrane ProteinsMethyltransferases

Identifiers

PMID18477614
PMCPMC2849272
OpenAlexW2038225007

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.