Localization of nascent RNA and CREB binding protein with the PML-containing nuclear body

LaMorte, Vickie J.; Dyck, Jacqueline A.; Ochs, Robert; Evans, Ronald M.

doi:10.1073/pnas.95.9.4991

Cited by 225 publications

(222 citation statements)

References 42 publications

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“…On the other hand, evidence for a direct spatial connection of genes to the PODs comes from a recent study showing that one marked gene locus is surrounded by a POD (Tsukamoto et al, 2000). However, whether the PODs represent actual sites of transcription remains controversial: while early work suggested the PODs contain nascent RNA (LaMorte et al, 1998) and RNA polymerase II (von Mikecz et al, 2000), one recent study did not detect a signi®cant amount of transcription inside the PODs, but in their immediate surrounding using high resolution techniques (Boisvert et al, 2000).…”

Section: The Relationship Between the Pods And Transcriptionmentioning

confidence: 99%

Transcriptional regulation in acute promyelocytic leukemia

et al. 2001

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Section: The Relationship Between the Pods And Transcriptionmentioning

confidence: 99%

Transcriptional regulation in acute promyelocytic leukemia

et al. 2001

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“…The composition of PML bodies is heterogeneous with several components present only in a subset of bodies (Carlile et al, 1998;LaMorte et al, 1998;Borden et al, 1998b). PML associated with proteins involved in translation and transcription (Melnick and Licht, 1999).…”

Section: Introductionmentioning

confidence: 99%

“…PML associated with proteins involved in translation and transcription (Melnick and Licht, 1999). mRNA is present in some but not all nuclear bodies (LaMorte et al, 1998). Apart from nuclear bodies, PML is found as a soluble component in the nucleus and a small fraction of PML is found in bodies in the cytoplasm (Flenghi et al, 1995).…”

Section: Introductionmentioning

confidence: 99%

The promyelocytic leukemia (PML) protein suppresses cyclin D1 protein production by altering the nuclear cytoplasmic distribution of cyclin D1 mRNA

2000

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The majority of the promyelocytic leukemia (PML) protein is present in nuclear bodies which are altered in several pathogenic conditions including acute promyelocytic leukemia. PML nuclear bodies are found in nearly all cells yet their function remains unknown. Here, we demonstrate that PML and the eukaryotic initiation factor 4E (eIF-4E) co-localize and co-immunopurify. eIF-4E is involved in nucleocytoplasmic transport of speci®c mRNAs including cyclin D1. eIF-4E overexpression leads to increased cyclin D1 protein levels; whereas, overexpression of PML leads to decreased cyclin D1 levels. Neither PML nor eIF-4E cause signi®cant changes in cyclin D1 mRNA levels. The association with eIF-4E led us to investigate if PML could alter mRNA distribution as a possible post-transcriptional mechanism for suppressing cyclin D1 production. We show that overexpression of PML results in nuclear retention of cyclin D1 mRNA and that intact PML nuclear bodies are required. Addition of eIF-4E overcomes PML induced retention and alters the morphology of PML bodies suggesting a mechanism by which eIF-4E can modulate PML function. These results raise the possibility that PML nuclear bodies may participate in the regulation of nucleocytoplasmic transport of speci®c mRNAs.

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“…PML nuclear bodies are altered by pathogenic conditions including APL and viral infection. The composition of PML bodies is heterogeneous with several components present only in some bodies (Carlile et al, 1998;Borden et al, 1998b;LaMorte et al, 1998). PML associates with over 15 proteins including factors involved in RNA transport, transcription and some ribosomal components (Melnick and Licht, 1999).…”

Section: Introductionmentioning

confidence: 99%

The promyelocytic leukemia protein PML interacts with the proline-rich homeodomain protein PRH: a RING may link hematopoiesis and growth control

et al. 1999

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Acute promyelocytic leukemia (APL) is characterized by a block in myeloid cell di erentiation. As a result of a chromosomal translocation in these patients, the promyelocytic leukemia protein PML is disrupted as are the nuclear bodies it forms. Disruption of PML and PML nuclear bodies in APL is linked to a loss of growth control and subsequent leukemogenesis. PML contains a zinc-binding domain known as the RING which is required for formation of these bodies. Using yeast 2-hybrid techniques, we found that PML and a related RING protein, Z, bind the proline rich homeodomain protein (PRH) through their RING domains. Previous reports indicate that PRH functions in hematopoiesis and may act as a transcriptional repressor. Our data indicate that PML and Z both bind the repressor domain of PRH and are the ®rst protein partners reported for PRH. We observe that PRH has a punctate pattern in both the nucleus and cytoplasm of chronic myelogenous leukemia K562 cells and in the APL cell line, NB4. Immunoprecipitation and co-localization studies indicate that PML and PRH interact in both cell lines. The e ect on cell growth by PML and the hematopoietic actions of PRH raises the possibility that the interaction between PML and PRH represents a link between growth control and hematopoiesis.

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Localization of nascent RNA and CREB binding protein with the PML-containing nuclear body

Cited by 225 publications

References 42 publications

Transcriptional regulation in acute promyelocytic leukemia

Transcriptional regulation in acute promyelocytic leukemia

The promyelocytic leukemia (PML) protein suppresses cyclin D1 protein production by altering the nuclear cytoplasmic distribution of cyclin D1 mRNA

The promyelocytic leukemia protein PML interacts with the proline-rich homeodomain protein PRH: a RING may link hematopoiesis and growth control

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