Evidence map›Paper›PMID 22303004›Full record

ArticleThe Journal of biological chemistry2012

Phosphorylation of Sar1b protein releases liver fatty acid-binding protein from multiprotein complex in intestinal cytosol enabling it to bind to endoplasmic reticulum (ER) and bud the pre-chylomicron transport vesicle.

Shahzad Siddiqi, Charles M Mansbach

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.1field-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

18 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Review
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  4. Article
  5. Review
  6. Sorting and Export of Proteins at the Endoplasmic Reticulum.Cold Spring Harbor perspectives in biology · 2023
    Review
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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

2 authors at 1 institution in 1 country.

Shahzad SiddiqiDepartment of Medicine, University of Tennessee Health Science Center, Memphis, Tennessee 38163 and.
Charles M MansbachDepartment of Medicine, University of Tennessee Health Science Center, Memphis, Tennessee 38163 and; Veterans Affairs Medical Center, Memphis, Tennessee 38104. Electronic address: cmansbach@uthsc.edu.
University of Tennessee Health Science Center · US

Funding

A Cell Biological Approach to Lipid Absorption.R01DK074565 · NIDDK · UNIVERSITY OF TENNESSEE HEALTH SCI CTR · PI MANSBACH, CHARLES MILTON · 2006 to 2010
$1.5M
NIDDK NIH HHS DK074565NIDDK NIH HHS R01 DK074565
6 · The paper itself

Abstract

Native cytosol requires ATP to initiate the budding of the pre-chylomicron transport vesicle from intestinal endoplasmic reticulum (ER). When FABP1 alone is used, no ATP is needed. Here, we test the hypothesis that in native cytosol FABP1 is present in a multiprotein complex that prevents FABP1 binding to the ER unless the complex is phosphorylated. We found on chromatography of native intestinal cytosol over a Sephacryl S-100 HR column that FABP1 (14 kDa) eluted in a volume suggesting a 75-kDa protein complex that contained four proteins on an anti-FABP1 antibody pulldown. The FABP1-containing column fractions were chromatographed over an anti-FABP1 antibody adsorption column. Proteins co-eluted from the column were identified as FABP1, Sar1b, Sec13, and small VCP/p97-interactive protein by immunoblot, LC-MS/MS, and MALDI-TOF. The four proteins of the complex had a total mass of 77 kDa and migrated on native PAGE at 75 kDa. When the complex was incubated with intestinal ER, there was no increase in FABP1-ER binding. However, when the complex member Sar1b was phosphorylated by PKCζ and ATP, the complex completely disassembled into its component proteins that migrated at their monomer molecular weight on native PAGE. FABP1, freed from the complex, was now able to bind to intestinal ER and generate the pre-chylomicron transport vesicle (PCTV). No increase in ER binding or PCTV generation was observed in the absence of PKCζ or ATP. We conclude that phosphorylation of Sar1b disrupts the FABP1-containing four-membered 75-kDa protein complex in cytosol enabling it to bind to the ER and generate PCTV.

Indexed as

Adenosine TriphosphateAnimalsBiological Transport, ActiveChylomicronsCytosolEndoplasmic ReticulumFatty Acid-Binding ProteinsIntestinal MucosaMaleMonomeric GTP-Binding ProteinsPhosphorylationProtein BindingProtein Kinase C-epsilonProtein PrecursorsRatsRats, Sprague-DawleyAdenosine TriphosphateChylomicronsFabp1 protein, ratFatty Acid-Binding ProteinsMonomeric GTP-Binding ProteinsProtein Kinase C-epsilonProtein Precursors

Identifiers

PMID22303004
PMCPMC3323000
OpenAlexW2084909613

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.