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PMID: 9794812 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Demonstration of a RNA-dependent nuclear interaction between the promyelocytic leukaemia protein and glyceraldehyde-3-phosphate dehydrogenase.

The Biochemical journal ·Vol. 335 ( Pt 3) ·1998-11-01 ·Pages 691-6

Carlile GW, Tatton WG, Borden KL

Abstract

The promyelocytic leukaemia (protein) (PML) localizes to multiprotein complexes known as PML nuclear bodies. We found that glyceraldehyde-3-phosphate dehydrogenase (GAPDH) co-immunoprecipitates with PML and co-localizes with PML in nuclear bodies. RNase treatment disrupts the ability of PML and GAPDH to both co-localize and co-immunoprecipitate, indicating that the association between PML and GAPDH depends on the presence of RNA. Disruption of PML bodies contributes towards reduced apoptosis in acute promyelocytic leukaemia and GAPDH induces apoptotic neuronal death. The GAPDH-PML interaction may be involved in the regulation of apoptosis.

MeSH Terms
3T3 Cells Animals Cell Line Cell Nucleus/metabolism Electrophoresis, Polyacrylamide Gel Fibroblasts Glyceraldehyde-3-Phosphate Dehydrogenases/isolation & purification,metabolism Humans Mice Neoplasm Proteins/isolation & purification,metabolism Nuclear Proteins/metabolism Promyelocytic Leukemia Protein RNA/metabolism Ribonucleases Transcription Factors/isolation & purification,metabolism Tumor Suppressor Proteins
Chemicals
Neoplasm Proteins Nuclear Proteins Pml protein, mouse Promyelocytic Leukemia Protein Transcription Factors Tumor Suppressor Proteins PML protein, human RNA Glyceraldehyde-3-Phosphate Dehydrogenases Ribonucleases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Carlile G W
Department of Physiology and Biophysics, Dalhousie University, Halifax, Nova Scotia, Canada.
Tatton W G
Borden K L
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Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
Published
1998-11-01
Pages
691-6
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1219833
Subset
IM
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