Evidence map›Paper›PMID 17493869›Full record

ArticleBiochimica et biophysica acta2007

Mitochondrial glycerol-3-P acyltransferase 1 is most active in outer mitochondrial membrane but not in mitochondrial associated vesicles (MAV).

Magalí Pellon-Maison, Mauro A Montanaro, Rosalind A Coleman, María R Gonzalez-Baró

Open access · greenAbstract read
In one paragraph

Article in Biochimica et biophysica acta, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
0.5field-weighted citation impact, top 32% 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

20 citing papers in PubMed, 31 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Review
  16. Phosphorylation and Acetylation of Acyl-CoA Synthetase- I.Journal of proteomics & bioinformatics · 2011
    Article
  17. Article
  18. Article
  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

4 authors at 2 institutions in 2 countries.

Magalí Pellon-MaisonInstituto de Investigaciones Bioquímicas de La Plata (CONICET-UNLP), 60 and 120, 1900 La Plata, Argentina.
Mauro A Montanaro
Rosalind A Coleman
María R Gonzalez-Baró
Consejo Nacional de Investigaciones Científicas y Técnicas · ARUniversity of North Carolina at Chapel Hill · US

Funding

METABOLISM OF GLYCEROLIPIDS IN LIVERR01DK056598 · NIDDK · UNIV OF NORTH CAROLINA CHAPEL HILL · PI COLEMAN, ROSALIND ANNE · 1999 to 2016
$5.0M
Regulation of mitochondrial glycerol-3-P acyltranferaseR03TW006034 · FIC · UNIVERSITY OF NORTH CAROLINA CHAPEL HILL · PI COLEMAN, ROSALIND ANNE · 2002 to 2004
$115k
FIC NIH HHS R03 TW006034FIC NIH HHS TW06034-01NIDDK NIH HHS DK52172NIDDK NIH HHS P30-DK350NIDDK NIH HHS R01 DK056598
6 · The paper itself

Abstract

Glycerol 3-phosphate acyltransferase-1 (GPAT1), catalyzes the committed step in phospholipid and triacylglycerol synthesis. Because both GPAT1 and carnitine-palmitoyltransferase 1 are located on the outer mitochondrial membrane (OMM) it has been suggested that their reciprocal regulation controls acyl-CoA metabolism at the OMM. To determine whether GPAT1, like carnitine-palmitoyltransferase 1, is enriched in both mitochondrial contact sites and OMM, and to correlate protein location and enzymatic function, we used Percoll and sucrose gradient fractionation of rat liver to obtain submitochondrial fractions. Most GPAT1 protein was present in a vesicular membrane fraction associated with mitochondria (MAV) but GPAT specific activity in this fraction was low. In contrast, highest GPAT1 specific activity was present in purified mitochondria. Contact sites from crude mitochondria, which contained markers for both endoplasmic reticulum (ER) and mitochondria, also showed high expression of GPAT1 protein but low specific activity, whereas contact sites isolated from purified mitochondria lacked ER markers and expressed highly active GPAT1. To determine how GPAT1 is targeted to mitochondria, recombinant protein was synthesized in vitro and its incorporation into crude and purified mitochondria was assayed. GPAT1 was rapidly incorporated into mitochondria, but not into microsomes. Incorporation was ATP-driven, and lack of GPAT1 removal by alkali and a chaotropic agent showed that GPAT1 had become an integral membrane protein after incorporation. These results demonstrate that two pools of GPAT1 are present in rat liver mitochondria: an active one, located in OMM and a less active one, located in membranes (ER-contact sites and mitochondrial associated vesicles) associated with both mitochondria and ER.

Indexed as

Adenosine TriphosphateAnimalsBiomarkersCell FractionationComplex MixturesEndoplasmic ReticulumGlycerol-3-Phosphate O-AcyltransferaseMaleMitochondria, LiverMitochondrial MembranesProtein TransportRatsRats, WistarSubmitochondrial ParticlesAdenosine TriphosphateBiomarkersComplex MixturesGlycerol-3-Phosphate O-Acyltransferase

Identifiers

PMID17493869
PMCPMC2230616
OpenAlexW1988525955

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.