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J. Biol. Chem., Vol. 279, Issue 42, 43799-43804, October 15, 2004

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TIN2 Mediates Functions of TRF2 at Human Telomeres^*

Sahn-ho Kim, Christian Beausejour, Albert R. Davalos, Patrick Kaminker¶, Seok-Jin Heo, and Judith Campisi||

From the Life Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, California 94720 and the ^¶Buck Institute for Age Research, Novato, California 94945

Telomeres are protective structures at chromosome ends and are crucial for genomic stability. Mammalian TRF1 and TRF2 bind the double-stranded telomeric repeat sequence and in turn are bound by TIN2, TANK1, TANK2, and hRAP1. TRF1 is a negative regulator of telomere length in telomerase-positive cells, whereas TRF2 is important for telomere capping. TIN2 was identified as a TRF1-interacting protein that mediates TRF1 function. We show here that TIN2 also interacts with TRF2 in vitro and in yeast and mammalian cells. TIN2 mutants defective in binding of TRF1 or TRF2 induce a DNA damage response and destabilize TRF1 and TRF2 at telomeres in human cells. Our findings suggest that the functions of TRF1 and TRF2 are linked by TIN2.

Received for publication, July 29, 2004

^* This work was supported by research grants from the Ellison Medical Foundation, National Institutes of Health Grant (AG09909), University of California Breast Cancer Research Program (7KB0151), and a NIA Training Grant (AG00266) from the National Institutes of Health. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Present address: Berlex BioSciences, 2600 Hilltop Dr., Richmond, CA 94804.

^|| To whom correspondence should be addressed: Lawrence Berkeley National Laboratory, 1 Cyclotron Rd., Mailstop 84-171, Berkeley, CA 94720. Tel.: 510-486-4416; Fax: 510-486-4545; E-mail: JCAMPISI{at}LBL.GOV.

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