Evidence map›Paper›PMID 26056309›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Phosphoregulatory protein 14-3-3 facilitates SAC1 transport from the endoplasmic reticulum.

Kanika Bajaj Pahuja, Jinzhi Wang, Anastasia Blagoveshchenskaya, Lillian Lim, M S Madhusudhan, Peter Mayinger, Randy Schekman

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

23 citing papers in PubMed, 49 citations in OpenAlex.

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  14. Phosphatidylinositol Kinases and Phosphatases inFrontiers in cellular and infection microbiology · 2019
    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

7 authors at 3 institutions in 3 countries.

Kanika Bajaj PahujaDepartment of Molecular and Cell Biology, University of California, Berkeley, CA 94720; Howard Hughes Medical Institute, University of California, Berkeley, CA 94720; bajajk@gene.com schekman@berkeley.edu.
Jinzhi WangDivision of Nephrology & Hypertension, Oregon Health and Science University, Portland, OR 97239;
Anastasia BlagoveshchenskayaDivision of Nephrology & Hypertension, Oregon Health and Science University, Portland, OR 97239;
Lillian LimDepartment of Molecular and Cell Biology, University of California, Berkeley, CA 94720;
M S MadhusudhanDepartment of Biology, Indian Institute of Science Education and Research, Pune 411008, India; Bioinformatics Institute, Singapore 136781; Department of Biological Sciences, National University of Singapore, Singapore 117543.
Peter MayingerDivision of Nephrology & Hypertension, Oregon Health and Science University, Portland, OR 97239;
Randy SchekmanDepartment of Molecular and Cell Biology, University of California, Berkeley, CA 94720; Howard Hughes Medical Institute, University of California, Berkeley, CA 94720; bajajk@gene.com schekman@berkeley.edu.
Oregon Health & Science University · USUniversity of California, Berkeley · USNational University of Singapore · SG

Funding

Cell growth-dependent control of secretion by lipid signalsR01GM084088 · NIGMS · OREGON HEALTH & SCIENCE UNIVERSITY · PI MAYINGER, PETER J · 2009 to 2012
$1.2M
Howard Hughes Medical InstituteNIGMS NIH HHS R01 GM084088Wellcome Trust
6 · The paper itself

Abstract

Most secretory cargo proteins in eukaryotes are synthesized in the endoplasmic reticulum and actively exported in membrane-bound vesicles that are formed by the cytosolic coat protein complex II (COPII). COPII proteins are assisted by a variety of cargo-specific adaptor proteins required for the concentration and export of secretory proteins from the endoplasmic reticulum (ER). Adaptor proteins are key regulators of cargo export, and defects in their function may result in disease phenotypes in mammals. Here we report the role of 14-3-3 proteins as a cytosolic adaptor in mediating SAC1 transport in COPII-coated vesicles. Sac1 is a phosphatidyl inositol-4 phosphate (PI4P) lipid phosphatase that undergoes serum dependent translocation between the endoplasmic reticulum and Golgi complex and controls cellular PI4P lipid levels. We developed a cell-free COPII vesicle budding reaction to examine SAC1 exit from the ER that requires COPII and at least one additional cytosolic factor, the 14-3-3 protein. Recombinant 14-3-3 protein stimulates the packaging of SAC1 into COPII vesicles and the sorting subunit of COPII, Sec24, interacts with 14-3-3. We identified a minimal sorting motif of SAC1 that is important for 14-3-3 binding and which controls SAC1 export from the ER. This LS motif is part of a 7-aa stretch, RLSNTSP, which is similar to the consensus 14-3-3 binding sequence. Homology models, based on the SAC1 structure from yeast, predict this region to be in the exposed exterior of the protein. Our data suggest a model in which the 14-3-3 protein mediates SAC1 traffic from the ER through direct interaction with a sorting signal and COPII.

Indexed as

14-3-3 ProteinsAnimalsChlorocebus aethiopsCOP-Coated VesiclesCOS CellsEndoplasmic ReticulumHeLa CellsHumansMembrane ProteinsProtein BindingRecombinant Proteins14-3-3 ProteinsMembrane ProteinsRecombinant ProteinsSac1 protein, mammalian14-3-3adaptor proteinCOPII vesiclesreconstitutionSAC1

Identifiers

PMID26056309
PMCPMC4485137
OpenAlexW1612371477

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.