Evidence map›Paper›PMID 21383012›Full record

ArticleThe Journal of biological chemistry2011

The adipophilin C terminus is a self-folding membrane-binding domain that is important for milk lipid secretion.

Brandi M Chong, Tanya D Russell, Jerome Schaack, David J Orlicky, Philip Reigan, Mark Ladinsky, James L McManaman

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. 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
3.9field-weighted citation impact, top 7% 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, 46 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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 1 country.

Brandi M ChongGraduate Program in Molecular Biology, Division of Basic Reproductive Science, University of Colorado Anschutz Medical Campus, Aurora, Colorado 80045, USA.
Tanya D Russell
Jerome Schaack
David J Orlicky
Philip Reigan
Mark Ladinsky
James L McManaman
University of Colorado Anschutz Medical Campus · USUniversity of Colorado Boulder · US

Funding

The functional role of microRNAs in the normal mammary glandP01HD038129 · NICHD · UNIVERSITY OF COLORADO DENVER · PI ANDERSON, STEVEN M · 2000 to 2015
$15.2M
MECHANISMS OF MILK LIPID SECRETIONR01HD045965 · NICHD · UNIVERSITY OF COLORADO DENVER · PI MCMANAMAN, JAMES LEWIS · 2004 to 2013
$2.8M
North Carolina Collaborative PPRU NetworkU10HD045962 · NICHD · DUKE UNIVERSITY · PI BENJAMIN, DANIEL K. · 2004 to 2009
$2.1M
NICHD NIH HHS 2R01-HD045962NICHD NIH HHS P01 HD038129NICHD NIH HHS P01-HD38129NICHD NIH HHS R01 HD045965NICHD NIH HHS U10 HD045962
6 · The paper itself

Abstract

Cytoplasmic lipid droplets (CLD) in mammary epithelial cells undergo secretion by a unique membrane envelopment process to produce milk lipids. Adipophilin (ADPH/Plin2), a member of the perilipin/PAT family of lipid droplet-associated proteins, is hypothesized to mediate CLD secretion through interactions with apical plasma membrane elements. We found that the secretion of CLD coated by truncated ADPH lacking the C-terminal region encoding a putative four-helix bundle structure was impaired relative to that of CLD coated by full-length ADPH. We used homology modeling and analyses of the solution and membrane binding properties of purified recombinant ADPH C terminus to understand how this region possibly mediates CLD secretion. Homology modeling supports the concept that the ADPH C terminus forms a four-helix bundle motif and suggests that this structure can form stable membrane bilayer interactions. Circular dichroism and protease mapping studies confirmed that the ADPH C terminus is an independently folding α-helical structure that is relatively resistant to urea denaturation. Liposome binding studies showed that the purified C terminus binds to phospholipid membranes through electrostatic dependent interactions, and cell culture studies documented that it localizes to the plasma membrane. Collectively, these data provide direct evidence that the ADPH C terminus forms a stable membrane binding helical structure that is important for CLD secretion. We speculate that interactions between the four-helix bundle of ADPH and membrane phospholipids may be an initial step in milk lipid secretion.

Indexed as

Cell MembraneMembrane ProteinsMilkPhospholipidsProtein FoldingAnimalsFemaleLactationMammary Glands, AnimalMembranes, ArtificialMiceModels, MolecularPerilipin-2Protein Structure, SecondaryProtein Structure, TertiaryMembrane ProteinsMembranes, ArtificialPerilipin-2PhospholipidsPlin2 protein, mouse

Identifiers

PMID21383012
PMCPMC3123092
OpenAlexW2051908555

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.