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Apoptin T108 phosphorylation is not required for its tumor-specific nuclear localization but partially affects its apoptotic activity
- Source :
- Biochemical and Biophysical Research Communications. 354:391-395
- Publication Year :
- 2007
- Publisher :
- Elsevier BV, 2007.
-
Abstract
- Apoptin, a chicken anemia virus-encoded protein, induces apoptosis in human tumor cells but not in normal cells. In addition, Apoptin also exhibits tumor-specific nuclear localization and tumor-specific phosphorylation on threonine 108 (T108). Here, we studied the effects of T108 phosphorylation on the tumor-specific nuclear localization and apoptotic activity of Apoptin. We first showed that a hemagglutinin (HA)-tagged Apoptin, but not the green fluorescent protein-fused Apoptin used in many previous studies, exhibited the same intracellular distribution pattern as native Apoptin. We then made and analyzed an HA-Apoptin mutant with its T108 phosphorylation site abolished. We found that Apoptin T108 phosphorylation is not required for its tumor-specific nuclear localization and abolishing the T108 phosphorylation of Apoptin does affect its apoptotic activity in tumor cells but only partially. Our results support the previous finding that Apoptin contains two distinct apoptosis domains located separately at the N- and C-terminal regions and suggest that the T108 phosphorylation may only be required for the apoptotic activity mediated through the C-terminal apoptosis domain.
- Subjects :
- Threonine
Green Fluorescent Proteins
Mutant
Biophysics
Hemagglutinin (influenza)
Apoptosis
Tumor cells
Biochemistry
Humans
Phosphorylation
Molecular Biology
Cell Nucleus
biology
Cell Biology
Molecular biology
Neoplasm Proteins
Protein Structure, Tertiary
Hemagglutinins
Amino Acid Substitution
biology.protein
Capsid Proteins
Nuclear localization sequence
Intracellular
HeLa Cells
Subjects
Details
- ISSN :
- 0006291X
- Volume :
- 354
- Database :
- OpenAIRE
- Journal :
- Biochemical and Biophysical Research Communications
- Accession number :
- edsair.doi.dedup.....55ba241603abcfd07b1272a8d1b1ee0b