Evidence map›Paper›PMID 25865481›Full record

ArticleCell2015

Substrates Control Multimerization and Activation of the Multi-Domain ATPase Motor of Type VII Secretion.

Oren S Rosenberg, Dustin Dovala, Xueming Li, Lynn Connolly, Anastasia Bendebury, Janet Finer-Moore, James Holton, Yifan Cheng, Robert M Stroud, Jeffery S Cox

Abstract read
In one paragraph

Article in Cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 77 papers.

0numbers the graph read from it
0cells of the map it votes in
77citing papers in PubMed
–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

77 citing papers in PubMed.

  1. Oral Actinobacteria sense and defend against parasitic epibionts.bioRxiv : the preprint server for biology · 2026
    Article
  2. Article
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  8. The PE/PPE family proteins ofFrontiers in immunology · 2025
    Review
  9. Article
  10. Article
  11. Deep mutational scanning of EccDbioRxiv : the preprint server for biology · 2024
    Article
  12. New insights into the domain of unknown function (DUF) of EccCActa crystallographica. Section D, Structural biology · 2024
    Article
  13. Structure of a tripartite protein complex that targets toxins to the type VII secretion system.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  14. Article
  15. Review
  16. Article
  17. Review
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  19. Article
  20. Article

17 more citing papers are in PubMed but not listed here.

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

10 authors.

Oren S RosenbergDivision of Infectious Diseases, Department of Medicine, UCSF Medical Center, University of California, San Francisco, San Francisco, CA 94143-0654, USA.
Dustin DovalaDepartment of Microbiology and Immunology, Program in Microbial Pathogenesis and Host Defense, University of California, San Francisco, San Francisco, CA 94158, USA.
Xueming LiSchool of Life Sciences, Tsinghua University, Beijing 100084, China.
Lynn ConnollyDivision of Infectious Diseases, Department of Medicine, UCSF Medical Center, University of California, San Francisco, San Francisco, CA 94143-0654, USA; Achaogen, Inc., South San Francisco, CA 94080, USA.
Anastasia BendeburyDepartment of Microbiology and Immunology, Program in Microbial Pathogenesis and Host Defense, University of California, San Francisco, San Francisco, CA 94158, USA.
Janet Finer-MooreDepartment of Biophysics and Biochemistry, University of California, San Francisco, San Francisco, CA 94158, USA.
James HoltonDepartment of Biophysics and Biochemistry, University of California, San Francisco, San Francisco, CA 94158, USA; Lawrence Berkeley National Laboratory, MS6-2100, Berkeley, CA 94720, USA.
Yifan ChengDepartment of Biophysics and Biochemistry, University of California, San Francisco, San Francisco, CA 94158, USA.
Robert M StroudDepartment of Biophysics and Biochemistry, University of California, San Francisco, San Francisco, CA 94158, USA.
Jeffery S CoxDepartment of Microbiology and Immunology, Program in Microbial Pathogenesis and Host Defense, University of California, San Francisco, San Francisco, CA 94158, USA. Electronic address: jeffery.cox@ucsf.edu.

Funding

The role of Listeria cyclic-di-AMP during infection and immunityP01AI063302 · NIAID · UNIVERSITY OF CALIFORNIA BERKELEY · PI COX, JEFFERY S · 2004 to 2025
$45.5M
X-ray Absorption Spectroscopy (XAS) pp.711-759P41GM103393 · NIGMS · STANFORD UNIVERSITY · PI HODGSON, KEITH O · 2012 to 2019
$30.6M
Project 6 (Holton)U54GM094625 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI STROUD, ROBERT M · 2010 to 2014
$8.0M
BIOLOGY OF INFECTIOUS DISEASES TRAINING PROGRAMT32AI007641 · NIAID · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI MATTHEW G DORSEY · 2000 to 2026
$6.9M
Molecular Basis for Transmembrane Conduction & SignalingR37GM024485 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI STROUD, ROBERT M · 2007 to 2016
$4.7M
Regulation of ESX-1 secretion and its role in M. tuberculosis virulenceR01AI081727 · NIAID · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI COX, JEFFERY S · 2010 to 2014
$2.0M
Structural and functional studies of M. tuberculosis type VII secretionK08AI091656 · NIAID · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI ROSENBERG, OREN S · 2011 to 2014
$516k
NIAID NIH HHS K08 AI091656NIAID NIH HHS K08AI091656NIAID NIH HHS P01 AI063302NIAID NIH HHS P01AI063302NIAID NIH HHS R01 AI081727NIAID NIH HHS R01AI081727NIAID NIH HHS T32 AI007641NIGMS NIH HHS P41 GM103393NIGMS NIH HHS P41GM103393NIGMS NIH HHS R37 GM024485NIGMS NIH HHS U54 GM094625NIGMS NIH HHS U54GM094625
6 · The paper itself

Abstract

Mycobacterium tuberculosis and Staphylococcus aureus secrete virulence factors via type VII protein secretion (T7S), a system that intriguingly requires all of its secretion substrates for activity. To gain insights into T7S function, we used structural approaches to guide studies of the putative translocase EccC, a unique enzyme with three ATPase domains, and its secretion substrate EsxB. The crystal structure of EccC revealed that the ATPase domains are joined by linker/pocket interactions that modulate its enzymatic activity. EsxB binds via its signal sequence to an empty pocket on the C-terminal ATPase domain, which is accompanied by an increase in ATPase activity. Surprisingly, substrate binding does not activate EccC allosterically but, rather, by stimulating its multimerization. Thus, the EsxB substrate is also an integral T7S component, illuminating a mechanism that helps to explain interdependence of substrates, and suggests a model in which binding of substrates modulates their coordinate release from the bacterium.

Indexed as

Bacterial Secretion SystemsActinobacteriaAdenosine TriphosphatasesCrystallography, X-RayModels, MolecularMycobacterium tuberculosisStaphylococcus aureusVirulence FactorsAdenosine TriphosphatasesBacterial Secretion SystemsVirulence Factors

Identifiers

PMID25865481
PMCPMC4409929

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Registered trials

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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.