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https://hdl.handle.net/2440/7436
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Full metadata record
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dc.contributor.author | Lyons, R. | - |
dc.contributor.author | Deane, R. | - |
dc.contributor.author | Lynch, D. | - |
dc.contributor.author | Ye, Z. | - |
dc.contributor.author | Sanderson, G. | - |
dc.contributor.author | Eyre, H. | - |
dc.contributor.author | Sutherland, G. | - |
dc.contributor.author | Daly, R. | - |
dc.date.issued | 2001 | - |
dc.identifier.citation | Journal of Biological Chemistry, 2001; 276(20):17172-17180 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.issn | 1083-351X | - |
dc.identifier.uri | http://hdl.handle.net/2440/7436 | - |
dc.description.abstract | Tankyrase 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. | - |
dc.language.iso | en | - |
dc.publisher | Amer Soc Biochemistry Molecular Biology Inc | - |
dc.source.uri | http://dx.doi.org/10.1074/jbc.m009756200 | - |
dc.subject | Cell Line | - |
dc.subject | Chromosomes, Human, Pair 10 | - |
dc.subject | Humans | - |
dc.subject | Saccharomyces cerevisiae | - |
dc.subject | Glutathione Transferase | - |
dc.subject | Poly(ADP-ribose) Polymerases | - |
dc.subject | Tankyrases | - |
dc.subject | Adaptor Proteins, Signal Transducing | - |
dc.subject | Proteins | - |
dc.subject | Recombinant Fusion Proteins | - |
dc.subject | Chromatography, Affinity | - |
dc.subject | In Situ Hybridization, Fluorescence | - |
dc.subject | Chromosome Mapping | - |
dc.subject | Cloning, Molecular | - |
dc.subject | Sequence Alignment | - |
dc.subject | Binding Sites | - |
dc.subject | Amino Acid Sequence | - |
dc.subject | Sequence Homology, Amino Acid | - |
dc.subject | Gene Library | - |
dc.subject | Molecular Sequence Data | - |
dc.title | Identification of a novel human tankyrase through its interaction with the adaptor protein Grb14 | - |
dc.type | Journal article | - |
dc.identifier.doi | 10.1074/jbc.M009756200 | - |
pubs.publication-status | Published | - |
Appears in Collections: | Aurora harvest 5 Paediatrics publications |
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