Evidence map›Paper›PMID 18606141›Full record

ArticleDevelopmental cell2008

Two distinct modes of ESCRT-III recognition are required for VPS4 functions in lysosomal protein targeting and HIV-1 budding.

Collin Kieffer, Jack J Skalicky, Eiji Morita, Ivana De Domenico, Diane M Ward, Jerry Kaplan, Wesley I Sundquist

Abstract read
In one paragraph

Article in Developmental cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 114 papers.

0numbers the graph read from it
0cells of the map it votes in
114citing 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

114 citing papers in PubMed.

  1. Article
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  12. Insights into the function of ESCRT complex and LBPA in ASFV infection.Frontiers in cellular and infection microbiology · 2023
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. The Role of Exosome and the ESCRT Pathway on Enveloped Virus Infection.International journal of molecular sciences · 2021
    Review
  19. Article
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

Collin KiefferDepartment of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT 84112-5650, USA.
Jack J Skalicky
Eiji Morita
Ivana De Domenico
Diane M Ward
Jerry Kaplan
Wesley I Sundquist

Funding

X-ray Cryst. CoreP50GM082545 · NIGMS · UNIVERSITY OF UTAH · PI SUNDQUIST, WESLEY I. · 2007 to 2018
$51.1M
Biochemistry of HIV-1 Membrane Recognition and BuddingR01AI051174 · NIAID · UNIVERSITY OF UTAH · PI SUNDQUIST, WESLEY I. · 2002 to 2016
$7.2M
Structural biology of HIV buddingP01GM066521 · NIGMS · UNIVERSITY OF UTAH · PI SUNDQUIST, WESLEY IAN · 2002 to 2006
$6.6M
Biochemistry of HIV-1 BuddingR37AI051174 · NIAID · UTAH STATE HIGHER EDUCATION SYSTEM--UNIVERSITY OF UTAH · PI WESLEY I. SUNDQUIST · 2017 to 2026
$5.6M
Mechanism and Regulation of Iron Export by FerroportinR01DK070947 · NIDDK · UNIVERSITY OF UTAH · PI KAPLAN, JERRY · 2005 to 2014
$3.7M
RECEPTOR MEDIATED ENDOCYTOSIS IN ALVEOLAR MACROPHAGESR37HL026922 · NHLBI · UNIVERSITY OF UTAH · PI KAPLAN, JERRY · 1997 to 2006
$2.5M
RECEPTOR MEDIATED ENDOCYTOSIS IN ALVEOLAR MACROPHAGESR01HL026922 · NHLBI · UNIVERSITY OF UTAH · PI WARD, DIANE MCVEY · 1985 to 2012
$1.9M
NHLBI NIH HHS HL26922NHLBI NIH HHS R01 HL026922NHLBI NIH HHS R37 HL026922NIAID NIH HHS AI51174NIAID NIH HHS R01 AI051174NIAID NIH HHS R37 AI051174NIDDK NIH HHS DK070947NIDDK NIH HHS R01 DK070947NIGMS NIH HHS GM082545NIGMS NIH HHS P01 GM066521NIGMS NIH HHS P50 GM082545
6 · The paper itself

Abstract

The ESCRT pathway mediates membrane remodeling during enveloped virus budding, cytokinesis, and intralumenal endosomal vesicle formation. Late in the pathway, a subset of membrane-associated ESCRT-III proteins display terminal amphipathic "MIM1" helices that bind and recruit VPS4 ATPases via their MIT domains. We now report that VPS4 MIT domains also bind a second, "MIM2" motif found in a different subset of ESCRT-III subunits. The solution structure of the VPS4 MIT-CHMP6 MIM2 complex revealed that MIM2 elements bind in extended conformations along the groove between the first and third helices of the MIT domain. Mutations that block VPS4 MIT-MIM2 interactions inhibit VPS4 recruitment, lysosomal protein targeting, and HIV-1 budding. MIT-MIM2 interactions appear to be common throughout the ESCRT pathway and possibly elsewhere, and we suggest how these interactions could contribute to a mechanism in which VPS4 and ESCRT-III proteins function together to constrict the necks of budding vesicles.

Indexed as

Adenosine TriphosphatasesAmino Acid MotifsAmino Acid SequenceBinding SitesBiosensing TechniquesConserved SequenceHIV-1HumansLysosomesModels, BiologicalModels, MolecularMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularProtein BindingProtein ConformationProtein Interaction MappingAdenosine TriphosphatasesRecombinant ProteinsVesicular Transport Proteins

Identifiers

PMID18606141
PMCPMC2586299

What OpenQuestion holds

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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.