Evidence map›Paper›PMID 19342671›Full record

ArticleJournal of immunology (Baltimore, Md. : 1950)2009

A novel hybrid yeast-human network analysis reveals an essential role for FNBP1L in antibacterial autophagy.

Alan Huett, Aylwin Ng, Zhifang Cao, Petric Kuballa, Masaaki Komatsu, Mark J Daly, Daniel K Podolsky, Ramnik J Xavier

Abstract read
In one paragraph

Article in Journal of immunology (Baltimore, Md. : 1950), 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed, 2 pooled it
–field-weighted citation impact
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

38 citing papers in PubMed, 2 syntheses or guidelines pooled it.

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  10. Inhibition of the ULK1 protein complex suppressesThe Journal of biological chemistry · 2019
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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

8 authors.

Alan HuettCenter for Computational and Integrative Biology, MassachusettsGeneral Hospital, Harvard Medical School, Boston, MA 02114, USA.
Aylwin Ng
Zhifang Cao
Petric Kuballa
Masaaki Komatsu
Mark J Daly
Daniel K Podolsky
Ramnik J Xavier

Funding

Pilot & Feasibility ProgramP30DK043351 · NIDDK · MASSACHUSETTS GENERAL HOSPITAL · PI RAYMOND T CHUNG · 1991 to 2026
$35.3M
ROLE OF DIETARY CONSTITUENTS ON GENE EXPRESSION IN INTESTINAL EPITHELIUMP30DK040561 · NIDDK · MASSACHUSETTS GENERAL HOSPITAL · PI CHRISTOPHER P DUGGAN · 1994 to 2026
$31.6M
Toll-like Receptors and the Intestinal EpitheliumR01DK060049 · NIDDK · MASSACHUSETTS GENERAL HOSPITAL · PI XAVIER, RAMNIK J · 2002 to 2011
$3.5M
Systems Biology of Crohn's DiseaseR01DK083756 · NIDDK · MASSACHUSETTS GENERAL HOSPITAL · PI DALY, MARK JOSEPH, XAVIER, RAMNIK J · 2008 to 2011
$1.5M
Genomic Approaches to Host-Pathogen InteractionsR01AI062773 · NIAID · MASSACHUSETTS GENERAL HOSPITAL · PI XAVIER, RAMNIK J · 2006 to 2009
$1.4M
NIAID NIH HHS AI062773NIAID NIH HHS R01 AI062773NIDDK NIH HHS DK043351NIDDK NIH HHS DK060049NIDDK NIH HHS DK83756NIDDK NIH HHS P30 DK040561NIDDK NIH HHS P30 DK043351NIDDK NIH HHS R01 DK060049NIDDK NIH HHS R01 DK083756
6 · The paper itself

Abstract

Autophagy is a conserved cellular process required for the removal of defective organelles, protein aggregates, and intracellular pathogens. We used a network analysis strategy to identify novel human autophagy components based upon the yeast interactome centered on the core yeast autophagy proteins. This revealed the potential involvement of 14 novel mammalian genes in autophagy, several of which have known or predicted roles in membrane organization or dynamics. We selected one of these membrane interactors, FNBP1L (formin binding protein 1-like), an F-BAR-containing protein (also termed Toca-1), for further study based upon a predicted interaction with ATG3. We confirmed the FNBP1L/ATG3 interaction biochemically and mapped the FNBP1L domains responsible. Using a functional RNA interference approach, we determined that FNBP1L is essential for autophagy of the intracellular pathogen Salmonella enterica serovar Typhimurium and show that the autophagy process serves to restrict the growth of intracellular bacteria. However, FNBP1L appears dispensable for other forms of autophagy induced by serum starvation or rapamycin. We present a model where FNBP1L is essential for autophagy of intracellular pathogens and identify FNBP1L as a differentially used molecule in specific autophagic contexts. By using network biology to derive functional biological information, we demonstrate the utility of integrated genomics to novel molecule discovery in autophagy.

Indexed as

AutophagyAutophagy-Related ProteinsCarrier ProteinsCell LineComputational BiologyGene DeletionGene Expression RegulationHumansIntracellular SpaceProtein BindingRNA, Small InterferingSaccharomyces cerevisiaeSalmonella typhimuriumSubstrate SpecificityUbiquitinUbiquitin-Conjugating EnzymesATG3 protein, humanAutophagy-Related ProteinsCarrier ProteinsFNBP1L protein, humanRNA, Small InterferingUbiquitinUbiquitin-Conjugating Enzymes

Identifiers

PMID19342671
PMCPMC2752416

What OpenQuestion holds

Textmetadata
LicenceTDM
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.