Modulation of the Zac1's transactivation and coactivation functions via PML and Daxx within distinct subcellular localizations

Ching-Liang Ho; Yu-Chi Huang; Chien-Kuo Tai; Shu-Ting Liu; Jehng-Kang Wang; Wei-Ming Wang; Shih-Ming Huang

doi:10.1016/j.biocel.2010.01.020

Modulation of the Zac1's transactivation and coactivation functions via PML and Daxx within distinct subcellular localizations

Int J Biochem Cell Biol. 2010 Jun;42(6):902-10. doi: 10.1016/j.biocel.2010.01.020. Epub 2010 Jan 25.

Authors

Ching-Liang Ho¹, Yu-Chi Huang, Chien-Kuo Tai, Shu-Ting Liu, Jehng-Kang Wang, Wei-Ming Wang, Shih-Ming Huang

Affiliation

¹ Department of Medicine, Division of Hematology/Oncology, Tri-Service General Hospital, National Defense Medical Center, Taipei, 114, Taiwan, ROC. [email protected]

PMID: 20097304
DOI: 10.1016/j.biocel.2010.01.020

Abstract

Zac1 acts as a transcription factor and a transcriptional cofactor cooperated with histone acetyltransferases and/or histone deacetylases. The molecular mechanisms underlying the subcellular localization and specificity of Zac1 transcriptional regulation are unclear. Here, we show that Zac1 might have physical and functional interactions with death-associated protein (Daxx) and promyelocytic leukemia protein (PML). However, unlike Daxx, nuclear Zac1 was not relocalized into PML nuclear bodies (PML-NBs). The enhancement of the transactivation activity of Zac1 by PML and Daxx might occur outside PML-NBs. Other components of PML-NBs, such as CREB-binding protein (CBP), ubiquitin-conjugating enzyme 9, and p53, were also regulatory targets for Zac1, for whom the locations to mediate its regulatory functions were distinct from PML-NBs. Our findings further suggest that Zac1 might play differential roles over the functions of CBP depending on the status of post-translational modification on CBP. Hence, our results link PML-NB components to the transactivation and coactivation functions of Zac1 at non-PML-NB sites.

Publication types

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

MeSH terms

Active Transport, Cell Nucleus
Adaptor Proteins, Signal Transducing / genetics
Adaptor Proteins, Signal Transducing / metabolism*
CREB-Binding Protein / metabolism
Cell Cycle Proteins / genetics
Cell Cycle Proteins / metabolism*
Cell Nucleus / metabolism*
Cloning, Molecular
Co-Repressor Proteins
Fluorescent Antibody Technique
HeLa Cells
Humans
Intranuclear Inclusion Bodies / metabolism*
Molecular Chaperones
Nuclear Proteins / genetics
Nuclear Proteins / metabolism*
Promyelocytic Leukemia Protein
Protein Binding
Protein Transport
Transcription Factors / genetics
Transcription Factors / metabolism*
Transcriptional Activation
Tumor Suppressor Protein p53 / metabolism
Tumor Suppressor Proteins / genetics
Tumor Suppressor Proteins / metabolism*
Ubiquitin-Conjugating Enzymes / metabolism

Substances

Adaptor Proteins, Signal Transducing
Cell Cycle Proteins
Co-Repressor Proteins
DAXX protein, human
Molecular Chaperones
Nuclear Proteins
PLAGL1 protein, human
Promyelocytic Leukemia Protein
Transcription Factors
Tumor Suppressor Protein p53
Tumor Suppressor Proteins
PML protein, human
CREB-Binding Protein
Ubiquitin-Conjugating Enzymes