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Molecular and Cellular Biology, June 2004, p. 5314-5323, Vol. 24, No. 12
0270-7306/04/$08.00+0     DOI: 10.1128/MCB.24.12.5314-5323.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Vault Poly(ADP-Ribose) Polymerase Is Associated with Mammalian Telomerase and Is Dispensable for Telomerase Function and Vault Structure In Vivo

Yie Liu,1,2* Bryan E. Snow,1 Valerie A. Kickhoefer,3 Natalie Erdmann,1 Wen Zhou,4 Andrew Wakeham,1 Marla Gomez,2 Leonard H. Rome,3,5 and Lea Harrington1,6*

Ontario Cancer Institute/Advanced Medical Discovery Institute, Toronto, Ontario M5G 2C1,1 Department of Medical Biophysics, University of Toronto, Toronto, Ontario M5G 2M9, Canada,6 Functional Genomics Group/Life Sciences Division, Oak Ridge National Laboratory, Oak Ridge, Tennessee 37831,2 Department of Biological Chemistry, David Geffen School of Medicine,3 Jonsson Comprehensive Cancer Center, University of California at Los Angeles, Los Angeles, California 90095,4 Amgen Inc., Thousand Oaks, California 913205

Received 26 December 2003/ Returned for modification 7 March 2004/ Accepted 22 March 2004

Vault poly(ADP-ribose) polymerase (VPARP) was originally identified as a minor protein component of the vault ribonucleoprotein particle, which may be involved in molecular assembly or subcellular transport. In addition to the association of VPARP with the cytoplasmic vault particle, subpopulations of VPARP localize to the nucleus and the mitotic spindle, indicating that VPARP may have other cellular functions. We found that VPARP was associated with telomerase activity and interacted with exogenously expressed telomerase-associated protein 1 (TEP1) in human cells. To study the possible role of VPARP in telomerase and vault complexes in vivo, mVparp-deficient mice were generated. Mice deficient in mVparp were viable and fertile for up to five generations, with no apparent changes in telomerase activity or telomere length. Vaults purified from mVparp-deficient mouse liver appeared intact, and no defect in association with other vault components was observed. Mice deficient in mTep1, whose disruption alone does not affect telomere function but does affect the stability of vault RNA, showed no additional telomerase or telomere-related phenotypes when the mTep1 deficiency was combined with an mVparp deficiency. These data suggest that murine mTep1 and mVparp, alone or in combination, are dispensable for normal development, telomerase catalysis, telomere length maintenance, and vault structure in vivo.

* Corresponding author: Mailing address for Yie Liu: Life Sciences Division, Oak Ridge National Laboratory, Bethel Valley Rd., P.O. Box 2008, Building 1061, Room 208, Oak Ridge, TN 37831-6445. Phone: (865) 574-5396. Fax: (865) 574-5345. E-mail: liuy3{at}ornl.gov. Mailing address for Lea Harrington: Ontario Cancer Institute/Advanced Medical Discovery Institute, 620 University Ave., Toronto, Ontario M5G 2C1, Canada. Phone: (416) 946-2834. Fax: (416) 204-2277. E-mail: leah{at}uhnres.utoronto.ca.

Molecular and Cellular Biology, June 2004, p. 5314-5323, Vol. 24, No. 12
0022-538X/04/$08.00+0     DOI: 10.1128/MCB.24.12.5314-5323.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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