Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/7436
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dc.contributor.authorLyons, R.en
dc.contributor.authorDeane, R.en
dc.contributor.authorLynch, D.en
dc.contributor.authorYe, Z.en
dc.contributor.authorSanderson, G.en
dc.contributor.authorEyre, H.en
dc.contributor.authorSutherland, G.en
dc.contributor.authorDaly, R.en
dc.date.issued2001en
dc.identifier.citationJournal of Biological Chemistry, 2001; 276(20):17172-17180en
dc.identifier.issn0021-9258en
dc.identifier.issn1083-351Xen
dc.identifier.urihttp://hdl.handle.net/2440/7436-
dc.description.abstractTankyrase is an ankyrin repeat-containing poly(ADP-ribose) polymerase originally isolated as a binding partner for the telomeric protein TRF1, but recently identified as a mitogen-activated protein kinase substrate implicated in regulation of Golgi vesicle trafficking. In this study, a novel human tankyrase, designated tankyrase 2, was isolated in a yeast two-hybrid screen as a binding partner for the Src homology 2 domain-containing adaptor protein Grb14. Tankyrase 2 is a 130-kDa protein, which lacks the N-terminal histidine/proline/serine-rich region of tankyrase, but contains a corresponding ankyrin repeat region, sterile alpha motif module, and poly(ADP-ribose) polymerase homology domain. The TANKYRASE 2 gene localizes to chromosome 10q23.2 and is widely expressed, with mRNA transcripts particularly abundant in skeletal muscle and placenta. Upon subcellular fractionation, both Grb14 and tankyrase 2 associate with the low density microsome fraction, and association of these proteins in vivo can be detected by co-immunoprecipitation analysis. Deletion analyses implicate the N-terminal 110 amino acids of Grb14 and ankyrin repeats 10-19 of tankyrase 2 in mediating this interaction. This study supports a role for the tankyrases in cytoplasmic signal transduction pathways and suggests that vesicle trafficking may be involved in the subcellular localization or signaling function of Grb14.en
dc.language.isoenen
dc.publisherAmer Soc Biochemistry Molecular Biology Incen
dc.subjectCell Line; Chromosomes, Human, Pair 10; Humans; Saccharomyces cerevisiae; Glutathione Transferase; Poly(ADP-ribose) Polymerases; Tankyrases; Adaptor Proteins, Signal Transducing; Proteins; Recombinant Fusion Proteins; Chromatography, Affinity; In Situ Hybridization, Fluorescence; Chromosome Mapping; Cloning, Molecular; Sequence Alignment; Binding Sites; Amino Acid Sequence; Sequence Homology, Amino Acid; Gene Library; Molecular Sequence Dataen
dc.titleIdentification of a novel human tankyrase through its interaction with the adaptor protein Grb14en
dc.typeJournal articleen
dc.identifier.rmid0020010923en
dc.identifier.doi10.1074/jbc.M009756200en
dc.identifier.pubid61699-
pubs.library.collectionPaediatrics publicationsen
pubs.verification-statusVerifieden
pubs.publication-statusPublisheden
Appears in Collections:Paediatrics publications

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