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Originally published In Press as doi:10.1074/jbc.M009756200 on February 22, 2001

J. Biol. Chem., Vol. 276, Issue 20, 17172-17180, May 18, 2001
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Identification of a Novel Human Tankyrase through Its Interaction with the Adaptor Protein Grb14*

Ruth J. LyonsDagger , Róisín DeaneDagger , Danielle K. LynchDagger , Zheng-Sheng Jeffrey Ye§, Georgina M. SandersonDagger , Helen J. Eyre||, Grant R. Sutherland||, and Roger J. DalyDagger **

From the Dagger  Cancer Research Program, Garvan Institute of Medical Research, St. Vincent's Hospital, Sydney, New South Wales 2010, Australia, the § Department of Cell Biology and Genetics, Rockefeller University, New York, New York 10021, the  Department of Medicine, Memorial Sloan-Kettering Cancer Center, New York, New York 10021, and the || Centre for Medical Genetics, Department of Cytogenetics and Molecular Genetics, Women's and Children's Hospital, Adelaide, South Australia 5006, Australia

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.

* This work was funded by research grants from the National Health and Medical Research Council of Australia, the New South Wales Cancer Council, and the Kathleen Cuningham Foundation.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF329696.

** To whom correspondence should be addressed. Tel.: 61-2-9295-8333; Fax: 61-2-9295-8321; E-mail: r.daly@garvan.org.au.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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