Back to Search
Start Over
The promyelocytic leukemia gene product (PML) forms stable complexes with the retinoblastoma protein.
- Source :
-
Molecular and cellular biology [Mol Cell Biol] 1998 Feb; Vol. 18 (2), pp. 1084-93. - Publication Year :
- 1998
-
Abstract
- PML is a nuclear protein with growth-suppressive properties originally identified in the context of the PML-retinoic acid receptor alpha (RAR alpha) fusion protein of acute promyelocytic leukemia. PML localizes within distinct nuclear structures, called nuclear bodies, which are disrupted by the expression of PML-RAR alpha. We report that PML colocalizes with the nonphosphorylated fraction of the retinoblastoma protein (pRB) within nuclear bodies and that pRB is delocalized by PML-RAR alpha expression. Both PML and PML-RAR alpha form complexes with the nonphosphorylated form of pRB in vivo, and they interact with the pocket region of pRB. The regions of PML and PML-RAR alpha involved in pRB binding differ; in fact, the B boxes and the C-terminal region of PML, the latter of which is not present in PML-RAR alpha, are essential for the formation of stable complexes with pRB. Functionally, PML abolishes activation of glucocorticoid receptor-regulated transcription by pRB, whereas PML-RAR alpha further increases it. Our results suggest that PML may be part of transcription-regulatory complexes and that the oncogenic potential of the PML-RAR alpha protein may derive from the alteration of PML-regulated transcription.
- Subjects :
- Cell Division
Humans
Inclusion Bodies metabolism
Macromolecular Substances
Neoplasm Proteins genetics
Promoter Regions, Genetic
Promyelocytic Leukemia Protein
Protein Binding
Receptors, Glucocorticoid metabolism
Transcription Factors genetics
Transcription, Genetic
Tumor Cells, Cultured
Tumor Suppressor Proteins
Neoplasm Proteins metabolism
Nuclear Proteins
Oncogene Proteins, Fusion metabolism
Retinoblastoma Protein metabolism
Transcription Factors metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0270-7306
- Volume :
- 18
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Molecular and cellular biology
- Publication Type :
- Academic Journal
- Accession number :
- 9448006
- Full Text :
- https://doi.org/10.1128/MCB.18.2.1084