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J. Biol. Chem., Vol. 277, Issue 16, 14116-14126, April 19, 2002
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and
From The Skirball Institute of Biomolecular Medicine, New York
University School of Medicine, New York, New York 10016
Tankyrase 1, a human telomeric poly(ADP-ribose)
polymerase, was originally identified through its interaction with
TRF1, a negative regulator of telomere length. Tankyrase 1 ADP-ribosylates TRF1 in vitro, and its overexpression
induces telomere elongation in human cancer cells. In addition to its
telomeric localization, tankyrase 1 resides at multiple subcellular
sites, suggesting additional functions for this protein. Here we
identify TAB182, a novel tankyrase 1-binding protein of 182 kDa. TAB182
displays a complex pattern of subcellular localization. TAB182
localizes to the nucleus in a heterochromatic staining pattern and to
the cytoplasm, where it co-stains with the cortical actin network. TAB182 coimmunoprecipitates with tankyrase 1 from human cells and
serves as an acceptor of poly(ADP-ribosyl)ation by tankyrase 1 in
vitro. Like TRF1, TAB182 binds to the ankyrin domain (comprising 24 ankyrin repeats) of tankyrase 1. Surprisingly, dissection of this
domain reveals multiple discrete and overlapping binding sites for TRF1
and TAB182. Thus, we demonstrate five well conserved ankyrin repeat
clusters in tankyrase 1. Although each of the five ankyrin repeat
clusters independently binds to TRF1, only three of the five bind
toTAB182. These findings suggest that tankyrase 1 may act as a scaffold
for large molecular mass complexes made up of multiple binding
proteins. We discuss potential roles for tankyrase 1-mediated higher
order complexes at telomeres and at other subcellular sites.
Supported in part by The National Cancer Institute, Japanese
Foundation for Cancer Research Scientist Exchange Program. Present address: Division of Experimental Chemotherapy, Cancer Chemotherapy Center, Japanese Foundation for Cancer Research, 1-37-1 Kami-Ikebukuro, Toshima-ku, Tokyo 170-8455, Japan.
§
Recipient of the Kimmel Scholar Award. To whom correspondence
should be addressed: Skirball Institute of Biomolecular Medicine, New
York University School of Medicine, 540 First Ave., 2nd Floor, New
York, NY 10016. Tel.: 212-263-2540; Fax: 212-263-5711; E-mail: smithsu@saturn.med.nyu.edu.
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