Document Detail


PML3 interacts with TRF1 and is essential for ALT-associated PML bodies assembly in U2OS cells.
MedLine Citation:
PMID:  19900757     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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:
Jian Yu; Jianping Lan; Chong Wang; Quan Wu; Yuanyuan Zhu; Xiaoyu Lai; Jie Sun; Changjiang Jin; He Huang
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2009-11-08
Journal Detail:
Title:  Cancer letters     Volume:  291     ISSN:  1872-7980     ISO Abbreviation:  Cancer Lett.     Publication Date:  2010 May 
Date Detail:
Created Date:  2010-04-05     Completed Date:  2010-04-23     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  7600053     Medline TA:  Cancer Lett     Country:  Ireland    
Other Details:
Languages:  eng     Pagination:  177-86     Citation Subset:  IM    
Affiliation:
The First Affiliated Hospital of Zhejiang University Medical School, Hangzhou 310003, China.
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MeSH Terms
Descriptor/Qualifier:
Cell Cycle
DNA, Complementary / genetics
Fluorescent Antibody Technique
Glutathione Transferase / metabolism
Humans
Kinetics
Leukemia, Promyelocytic, Acute / genetics,  metabolism,  pathology
Microsatellite Repeats
Nuclear Proteins / genetics,  metabolism*
Palatine Tonsil / metabolism
Protein Binding
RNA, Small Interfering / genetics
Recombinant Fusion Proteins / metabolism
Recombinant Proteins / metabolism
Reverse Transcriptase Polymerase Chain Reaction
Telomeric Repeat Binding Protein 1 / genetics*,  metabolism
Transcription Factors / genetics,  metabolism*
Tumor Suppressor Proteins / genetics,  metabolism*
Chemical
Reg. No./Substance:
0/DNA, Complementary; 0/Nuclear Proteins; 0/RNA, Small Interfering; 0/Recombinant Fusion Proteins; 0/Recombinant Proteins; 0/Telomeric Repeat Binding Protein 1; 0/Transcription Factors; 0/Tumor Suppressor Proteins; 143220-95-5/PML protein, human; EC 2.5.1.18/Glutathione Transferase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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