Journal
BIOCHIMIE
Volume 90, Issue 1, Pages 83-92Publisher
ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER
DOI: 10.1016/j.biochi.2007.07.012
Keywords
telomeres; tankyrase; PARPs
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Funding
- NATIONAL CANCER INSTITUTE [R01CA095099, R01CA116352] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [T32GM007238] Funding Source: NIH RePORTER
- NCI NIH HHS [R01 CA95099, R01 CA116352, R01 CA095099] Funding Source: Medline
- NIGMS NIH HHS [GM07238] Funding Source: Medline
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Telomeres have special needs; they require distinct mechanisms for their protection, replication, and separation at mitosis. A dedicated six-subunit protein complex termed shelterin attends to these needs. But shelterin cannot do it alone and often relies on recruits from other cellular locales. One such recruit is tankyrase 1, a poly(ADP-ribose) polymerase that is brought to telomeres by the shelterin DNA binding subunit TRF1, where it functions in telomere length regulation and sister chromatid separation. An understanding of how tankyrase 1 functions at telomeres has been confounded by its complexity; it localizes to multiple subcellular sites, it has many diverse binding partners, and it has a closely related homolog (tankyrase 2) with which it may functionally overlap. This review summarizes our current knowledge of tankyrases focusing on their localization, binding partners, and function. (c) 2007 Published by Elsevier Masson SAS.
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