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PML3 interacts with TRF1 and is essential for ALT-associated PML bodies assembly in U2OS cells.
Cancer Lett 2010; 291(2):177-86CL

Abstract

Telomerase-negative cancer cells maintain their telomeres by a mechanism known as alternative lengthening of telomeres (ALT) and achieve unlimited replicative potential. A hallmark of ALT cells is the recruitment of telomeres to promyelocytic leukemia (PML) bodies and formation of ALT-associated PML bodies (APBs). Although the exact molecular mechanism of APBs assembly remains unclear, APBs assembly requires telomere and PML body-associated proteins, including TRF1 and PML. Here, we report that PML3, one of PML isoforms, is involved in APBs formation. As a new binding protein of TRF1 (telomeric repeat binding factor 1), PML3 directly interacts with TRF1 and recruits TRF1 to PML bodies in U2OS cells. More notably, depletion of PML3 by small interfering RNA does not affect PML bodies formation, but inhibits the recruitment of both TRF1 and TRF2 to APBs. Further study shows that the recruitment of TRF1 to APBs depends on its interaction with a specific PML3 isoform. Thus, the interaction of PML3 with TRF1 is isoform specific and likely to be essential for APBs assembly in U2OS cells.

Authors+Show Affiliations

The First Affiliated Hospital of Zhejiang University Medical School, Hangzhou 310003, China.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

19900757

Citation

Yu, Jian, et al. "PML3 Interacts With TRF1 and Is Essential for ALT-associated PML Bodies Assembly in U2OS Cells." Cancer Letters, vol. 291, no. 2, 2010, pp. 177-86.
Yu J, Lan J, Wang C, et al. PML3 interacts with TRF1 and is essential for ALT-associated PML bodies assembly in U2OS cells. Cancer Lett. 2010;291(2):177-86.
Yu, J., Lan, J., Wang, C., Wu, Q., Zhu, Y., Lai, X., ... Huang, H. (2010). PML3 interacts with TRF1 and is essential for ALT-associated PML bodies assembly in U2OS cells. Cancer Letters, 291(2), pp. 177-86. doi:10.1016/j.canlet.2009.10.009.
Yu J, et al. PML3 Interacts With TRF1 and Is Essential for ALT-associated PML Bodies Assembly in U2OS Cells. Cancer Lett. 2010 May 28;291(2):177-86. PubMed PMID: 19900757.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - PML3 interacts with TRF1 and is essential for ALT-associated PML bodies assembly in U2OS cells. AU - Yu,Jian, AU - Lan,Jianping, AU - Wang,Chong, AU - Wu,Quan, AU - Zhu,Yuanyuan, AU - Lai,Xiaoyu, AU - Sun,Jie, AU - Jin,Changjiang, AU - Huang,He, Y1 - 2009/11/08/ PY - 2009/05/17/received PY - 2009/10/11/revised PY - 2009/10/13/accepted PY - 2009/11/11/entrez PY - 2009/11/11/pubmed PY - 2010/4/24/medline SP - 177 EP - 86 JF - Cancer letters JO - Cancer Lett. VL - 291 IS - 2 N2 - Telomerase-negative cancer cells maintain their telomeres by a mechanism known as alternative lengthening of telomeres (ALT) and achieve unlimited replicative potential. A hallmark of ALT cells is the recruitment of telomeres to promyelocytic leukemia (PML) bodies and formation of ALT-associated PML bodies (APBs). Although the exact molecular mechanism of APBs assembly remains unclear, APBs assembly requires telomere and PML body-associated proteins, including TRF1 and PML. Here, we report that PML3, one of PML isoforms, is involved in APBs formation. As a new binding protein of TRF1 (telomeric repeat binding factor 1), PML3 directly interacts with TRF1 and recruits TRF1 to PML bodies in U2OS cells. More notably, depletion of PML3 by small interfering RNA does not affect PML bodies formation, but inhibits the recruitment of both TRF1 and TRF2 to APBs. Further study shows that the recruitment of TRF1 to APBs depends on its interaction with a specific PML3 isoform. Thus, the interaction of PML3 with TRF1 is isoform specific and likely to be essential for APBs assembly in U2OS cells. SN - 1872-7980 UR - https://www.unboundmedicine.com/medline/citation/19900757/PML3_interacts_with_TRF1_and_is_essential_for_ALT_associated_PML_bodies_assembly_in_U2OS_cells_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0304-3835(09)00631-4 DB - PRIME DP - Unbound Medicine ER -