Evidence map›Paper›PMID 18511562›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2008

ALIX-CHMP4 interactions in the human ESCRT pathway.

John McCullough, Robert D Fisher, Frank G Whitby, Wesley I Sundquist, Christopher P Hill

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 147 papers.

0numbers the graph read from it
0cells of the map it votes in
147citing 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

147 citing papers in PubMed.

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87 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

5 authors.

John McCulloughDepartment of Biochemistry, University of Utah, Salt Lake City, UT 84112-5650, USA.
Robert D Fisher
Frank G Whitby
Wesley I Sundquist
Christopher P Hill

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
Biochemistry of HIV-1 BuddingR37AI051174 · NIAID · UTAH STATE HIGHER EDUCATION SYSTEM--UNIVERSITY OF UTAH · PI WESLEY I. SUNDQUIST · 2017 to 2026
$5.6M
NIAID NIH HHS AI051174NIAID NIH HHS R01 AI051174NIAID NIH HHS R37 AI051174NIGMS NIH HHS GM082534NIGMS NIH HHS P50 GM082545
6 · The paper itself

Abstract

The ESCRT pathway facilitates membrane fission events during enveloped virus budding, multivesicular body formation, and cytokinesis. To promote HIV budding and cytokinesis, the ALIX protein must bind and recruit CHMP4 subunits of the ESCRT-III complex, which in turn participate in essential membrane remodeling functions. Here, we report that the Bro1 domain of ALIX binds specifically to C-terminal residues of the human CHMP4 proteins (CHMP4A-C). Crystal structures of the complexes reveal that the CHMP4 C-terminal peptides form amphipathic helices that bind across the conserved concave surface of ALIX(Bro1). ALIX-dependent HIV-1 budding is blocked by mutations in exposed ALIX(Bro1) residues that help contribute to the binding sites for three essential hydrophobic residues that are displayed on one side of the CHMP4 recognition helix (M/L/IxxLxxW). The homologous CHMP1-3 classes of ESCRT-III proteins also have C-terminal amphipathic helices, but, in those cases, the three hydrophobic residues are arrayed with L/I/MxxxLxxL spacing. Thus, the distinct patterns of hydrophobic residues provide a "code" that allows the different ESCRT-III subunits to bind different ESCRT pathway partners, with CHMP1-3 proteins binding MIT domain-containing proteins, such as VPS4 and Vta1/LIP5, and CHMP4 proteins binding Bro1 domain-containing proteins, such as ALIX.

Indexed as

Virus AssemblyAdenosine TriphosphatasesAmino Acid SequenceATPases Associated with Diverse Cellular ActivitiesBinding SitesCalcium-Binding ProteinsCarrier ProteinsCell Cycle ProteinsCrystallography, X-RayEndosomal Sorting Complexes Required for TransportEndosomesHIV-1HumansMolecular Sequence DataMutationProtein Interaction MappingAdenosine TriphosphatasesATPases Associated with Diverse Cellular ActivitiesCalcium-Binding ProteinsCarrier ProteinsCell Cycle ProteinsCHMP4A protein, humanCHMP4B protein, humanEndosomal Sorting Complexes Required for TransportPDCD6IP protein, humanVacuolar Proton-Translocating ATPasesVesicular Transport ProteinsVPS4A protein, humanVTA1 protein, human

Identifiers

PMID18511562
PMCPMC2409388

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.