Evidence map›Paper›PMID 24965341›Full record

ArticleBMC bioinformatics2014

Identification and phylogenetic analyses of VASt, an uncharacterized protein domain associated with lipid-binding domains in Eukaryotes.

Mehdi Khafif, Ludovic Cottret, Claudine Balagué, Sylvain Raffaele

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Article in BMC bioinformatics, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

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20citing papers in PubMed
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3 · Its place in the literature

Who cites it

20 citing papers in PubMed.

  1. Article
  2. Article
  3. An origin for a eukaryotic lipid transfer protein fold in Asgard archaea.bioRxiv : the preprint server for biology · 2025
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  8. Courier service for phosphatidylinositol: PITPs deliver on demand.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2021
    Review
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4 · The record

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5 · Who and what money

Authors and funding

4 authors.

Mehdi Khafif
Ludovic Cottret
Claudine Balagué
Sylvain RaffaeleINRA, Laboratoire des Interactions Plantes-Microorganismes (LIPM), UMR441, 24 Chemin de Borde Rouge - Auzeville, CS52627, F31326 Castanet Tolosan Cedex, France. Sylvain.raffaele@toulouse.inra.fr.

Funding

European Research Council 336808
6 · The paper itself

Abstract

backgroundSeveral regulators of programmed cell death (PCD) in plants encode proteins with putative lipid-binding domains. Among them, VAD1 is a regulator of PCD propagation harboring a GRAM putative lipid-binding domain. However the function of VAD1 at the subcellular level is unknown and the domain architecture of VAD1 has not been analyzed in details.

resultsWe analyzed sequence conservation across the plant kingdom in the VAD1 protein and identified an uncharacterized VASt (VAD1 Analog of StAR-related lipid transfer) domain. Using profile hidden Markov models (profile HMMs) and phylogenetic analysis we found that this domain is conserved among eukaryotes and generally associates with various lipid-binding domains. Proteins containing both a GRAM and a VASt domain include notably the yeast Ysp2 cell death regulator and numerous uncharacterized proteins. Using structure-based phylogeny, we found that the VASt domain is structurally related to Bet v1-like domains.

conclusionWe identified a novel protein domain ubiquitous in Eukaryotic genomes and belonging to the Bet v1-like superfamily. Our findings open perspectives for the functional analysis of VASt-containing proteins and the characterization of novel mechanisms regulating PCD.

Indexed as

PhylogenyAmino Acid SequenceAnimalsConserved SequenceEukaryotaGenomeHumansLipid MetabolismLipidsModels, MolecularMolecular Sequence DataProteinsProtein Structure, TertiarySequence AlignmentStructural Homology, ProteinLipidsProteins

Identifiers

PMID24965341
PMCPMC4082322

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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.