Evidence map›Paper›PMID 24248333›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Phosphorylation of the Rab exchange factor Sec2p directs a switch in regulatory binding partners.

Danièle Stalder, Emi Mizuno-Yamasaki, Majid Ghassemian, Peter J Novick

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
2.8field-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

24 citing papers in PubMed, 35 citations in OpenAlex.

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  11. Moderate Expression ofApplied and environmental microbiology · 2017
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  18. Activation of Rab8 guanine nucleotide exchange factor Rabin8 by ERK1/2 in response to EGF signaling.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  19. Article
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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

4 authors at 1 institution in 1 country.

Danièle StalderDepartment of Cellular and Molecular Medicine and Department of Chemistry and Biochemistry, Biomolecular and Proteomics Mass Spectrometry Facility, University of California, San Diego, La Jolla, CA 92093.
Emi Mizuno-Yamasaki
Majid Ghassemian
Peter J Novick
University of California, San Diego · US

Funding

GENETICS OF SECRETION IN YEASTR01GM035370 · NIGMS · YALE UNIVERSITY · PI PETER Jay NOVICK · 1985 to 2026
$7.0M
Coordination of membrane traffic through rab GEF and GAP cascadesR01GM082861 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI NOVICK, PETER JAY · 2008 to 2020
$4.4M
Acquisition of an Orbitrap Elite with ETDS10OD021724 · OD · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI KOMIVES, ELIZABETH A. · 2016 to 2016
$600k
NIGMS NIH HHS GM82861NIGMS NIH HHS R01 GM035370NIGMS NIH HHS R01 GM082861NIH HHS S10 OD021724
6 · The paper itself

Abstract

Sec2p is a guanine nucleotide exchange factor that promotes exocytosis by activating the Rab GTPase Sec4p. Sec2p is highly phosphorylated, and we have explored the role of phosphorylation in the regulation of its function. We have identified three phosphosites and demonstrate that phosphorylation regulates the interaction of Sec2p with its binding partners Ypt32p, Sec15p, and phosphatidyl-inositol-4-phosphate. In its nonphosphorylated form, Sec2p binds preferentially to the upstream Rab, Ypt32p-GTP, thus forming a Rab guanine nucleotide exchange factor cascade that leads to the activation of the downstream Rab, Sec4p. The nonphosphorylated form of Sec2p also binds to the Golgi-associated phosphatidyl-inositol-4-phosphate, which works in concert with Ypt32p-GTP to recruit Sec2p to Golgi-derived secretory vesicles. In contrast, the phosphorylated form of Sec2p binds preferentially to Sec15p, a downstream effector of Sec4p and a component of the exocyst tethering complex, thus forming a positive-feedback loop that prepares the secretory vesicle for fusion with the plasma membrane. Our results suggest that the phosphorylation state of Sec2p can direct a switch in its regulatory binding partners that facilitates maturation of the secretory vesicle and helps to promote the directionality of vesicular transport.

Indexed as

Biological TransportElectrophoresis, Polyacrylamide GelGuanine Nucleotide Exchange FactorsImmunoprecipitationMicroscopy, ElectronMicroscopy, FluorescenceMutagenesis, Site-DirectedPhosphatidylinositol PhosphatesPhosphorylationProtein Bindingrab GTP-Binding ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTransport VesiclesVesicular Transport ProteinsGuanine Nucleotide Exchange Factorsphosphatidylinositol 4-phosphatePhosphatidylinositol Phosphatesrab GTP-Binding ProteinsSaccharomyces cerevisiae ProteinsSEC15 protein, S cerevisiaeSEC2 protein, S cerevisiaeVesicular Transport ProteinsYPT32 protein, S cerevisiaemembrane trafficphospho-regulationvesicle maturationyeast

Identifiers

PMID24248333
PMCPMC3864272
OpenAlexW2169846040

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.