Linked Life Data

9804769

Source:http://linkedlifedata.com/resource/pubmed/id/9804769

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
46
pubmed:dateCreated
1998-12-8
pubmed:abstractText
Bok (Bcl-2-related ovarian killer) is a proapoptotic Bcl-2 family protein identified in the ovary based on its dimerization with the antiapoptotic protein Mcl-1. In addition to the Bcl-2 homology (BH) domains 1 and 2 and the transmembrane sequence, Bok also has a BH3 domain believed to be important for dimerization with selective antiapoptotic Bcl-2 proteins and cell killing. We identified a splicing variant of Bok mRNA with a deletion of 43 residues from the full-length protein (Bok-L), leading to the fusion of the N-terminal-half of its BH3 domain to the C-terminal-half of the BH1 domain. Genomic analysis indicated that the Bok has five exons, and the short form of Bok (Bok-S) represents the splicing out of exon three during transcription. Although Bok-S retains the apoptosis-inducing activity in transfected cells, it has lost the ability to dimerize with antiapoptotic proteins in vitro. Additional BH3 domain mutations of Bok-L also led to defective heterodimerization without affecting its proapoptotic action. Furthermore, similar deletions for the related channel-forming proapoptotic Bax and Bak did not impair their cell killing ability. Thus, the naturally occurring Bok-S variant represents a new form of proapoptotic protein that induces cell killing without heterodimerization with antiapoptotic Bcl-2 proteins. This variant appears to contain the minimal module spanning BH1 and BH2 domains and the transmembrane sequence for apoptosis induction by channel-forming Bcl-2 proteins.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
13
pubmed:volume
273
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
30139-46
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:9804769-Alternative Splicing, pubmed-meshheading:9804769-Amino Acid Sequence, pubmed-meshheading:9804769-Animals, pubmed-meshheading:9804769-Apoptosis, pubmed-meshheading:9804769-Binding Sites, pubmed-meshheading:9804769-Carrier Proteins, pubmed-meshheading:9804769-Dimerization, pubmed-meshheading:9804769-Female, pubmed-meshheading:9804769-Membrane Proteins, pubmed-meshheading:9804769-Mice, pubmed-meshheading:9804769-Models, Biological, pubmed-meshheading:9804769-Molecular Sequence Data, pubmed-meshheading:9804769-Ovary, pubmed-meshheading:9804769-Proto-Oncogene Proteins, pubmed-meshheading:9804769-Proto-Oncogene Proteins c-bcl-2, pubmed-meshheading:9804769-Rats, pubmed-meshheading:9804769-Rats, Sprague-Dawley, pubmed-meshheading:9804769-Structure-Activity Relationship, pubmed-meshheading:9804769-Transfection, pubmed-meshheading:9804769-Uterus, pubmed-meshheading:9804769-bcl-2 Homologous Antagonist-Killer Protein, pubmed-meshheading:9804769-bcl-2-Associated X Protein
pubmed:year
1998
pubmed:articleTitle
A splicing variant of the Bcl-2 member Bok with a truncated BH3 domain induces apoptosis but does not dimerize with antiapoptotic Bcl-2 proteins in vitro.
pubmed:affiliation
Division of Reproductive Biology, Department of Gynecology and Obstetrics, Stanford University Medical School, Stanford, California 94305-5317, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.