Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/7436
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Type: Journal article
Title: Identification of a novel human tankyrase through its interaction with the adaptor protein Grb14
Author: Lyons, R.
Deane, R.
Lynch, D.
Ye, Z.
Sanderson, G.
Eyre, H.
Sutherland, G.
Daly, R.
Citation: Journal of Biological Chemistry, 2001; 276(20):17172-17180
Publisher: Amer Soc Biochemistry Molecular Biology Inc
Issue Date: 2001
ISSN: 0021-9258
1083-351X
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.
Keywords: Cell 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 Data
RMID: 0020010923
DOI: 10.1074/jbc.M009756200
Appears in Collections:Paediatrics publications

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