Abstract
The promyelocytic leukaemia (protein) (PML) localizes to multi-protein 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.
Original language | English (US) |
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Pages (from-to) | 691-696 |
Number of pages | 6 |
Journal | Biochemical Journal |
Volume | 335 |
Issue number | 3 |
DOIs | |
State | Published - Nov 1 1998 |
ASJC Scopus subject areas
- Biochemistry
- Molecular Biology
- Cell Biology