Linked Life Data

10833333

Source:http://linkedlifedata.com/resource/pubmed/id/10833333

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2000-7-19
pubmed:databankReference
pubmed:abstractText
Voltage-dependent anion channels (VDACs) are small, integral membrane proteins that traverse the outer mitochondrial membrane and conduct ATP and other small metabolites. They are known to bind several kinases of intermediary metabolism in a tissue-specific fashion, have been found in close association with the adenine nucleotide translocator of the inner mitochondrial membrane, and are hypothesized to form part of the mitochondrial permeability transition pore, which results in the release of cytochrome c at the onset of apoptotic cell death. VDACs are found throughout all strata of eukaryotic evolution and exhibit biophysical characteristics that are well conserved from yeast to mammals. The mammalian VDAC gene family consists of three isoforms, each of which shares approximately 70% sequence identity with the other two family members. Recently, we reported that a single codon (ATG) exon is alternatively spliced into the transcript of the type 3 voltage-dependent anion channel (VDAC3) in a tissue-specific fashion. This unusual splicing event was shown to be conserved between mouse and human, and we theorized that the spliced exon could lead to the creation of an alternative translational initiation site. Here we report that a highly specific polyclonal VDAC3 antibody was unable to detect the truncated protein isoform indicative of this putative downstream start site. From these in vivo studies, we conclude that the alternatively spliced exon results in the insertion of a single methionine residue at amino acid position 39 of the mature VDAC3 protein. Additionally, we have used a cross-species genomic sequence comparison to identify conserved regions that may be involved in the regulation of small exon splicing.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1096-7192
pubmed:author
pubmed:copyrightInfo
Copyright 2000 Academic Press.
pubmed:issnType
Print
pubmed:volume
70
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
69-74
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:10833333-Alternative Splicing, pubmed-meshheading:10833333-Animals, pubmed-meshheading:10833333-Antibody Specificity, pubmed-meshheading:10833333-Base Sequence, pubmed-meshheading:10833333-Brain, pubmed-meshheading:10833333-Conserved Sequence, pubmed-meshheading:10833333-DNA, pubmed-meshheading:10833333-Exons, pubmed-meshheading:10833333-Gene Expression Regulation, pubmed-meshheading:10833333-Humans, pubmed-meshheading:10833333-Male, pubmed-meshheading:10833333-Mice, pubmed-meshheading:10833333-Mitochondria, Muscle, pubmed-meshheading:10833333-Mitochondrial Membrane Transport Proteins, pubmed-meshheading:10833333-Molecular Sequence Data, pubmed-meshheading:10833333-Muscle, Skeletal, pubmed-meshheading:10833333-Porins, pubmed-meshheading:10833333-Protein Isoforms, pubmed-meshheading:10833333-RNA, Messenger, pubmed-meshheading:10833333-Sequence Alignment, pubmed-meshheading:10833333-Sequence Analysis, DNA, pubmed-meshheading:10833333-Sequence Homology, Nucleic Acid, pubmed-meshheading:10833333-Voltage-Dependent Anion Channels
pubmed:year
2000
pubmed:articleTitle
The tissue-specific, alternatively spliced single ATG exon of the type 3 voltage-dependent anion channel gene does not create a truncated protein isoform in vivo.
pubmed:affiliation
Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, TX 77030, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.