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Interaction with Ppil3 leads to the cytoplasmic localization of Apoptin in tumor cells
- Source :
- Biochemical and Biophysical Research Communications. 372:14-18
- Publication Year :
- 2008
- Publisher :
- Elsevier BV, 2008.
-
Abstract
- Apoptin, a small protein encoded by chicken anemia virus (CAV), induces cell death specifically in cancer cells. In normal cells, Apoptin remains in the cytoplasm; whereas in cancerous cells, it migrates into the nucleus and kills the cell. Cellular localization appears to be crucial. Through a yeast two-hybrid screen, we identified human Peptidyl-prolyl isomerase-like 3 (Ppil3) as one of the Apoptin-associated proteins. Ppil3 could bind Apoptin directly, and held Apoptin in cytoplasm even in tumor cells. We then demonstrated that the nuclearcytoplasmic distribution of Apoptin is related to the expression level of intrinsic Ppil3. Moreover, extrinsic modifying of Ppil3 levels also resulted in nuclearcytoplasmic shuffling of Apoptin. The Apoptin P109A mutant, located between the putative nuclear localization and export signals, could significantly impair the function of Ppil3. Our results suggest a new direction for the localization mechanism study of Apoptin in cells.
- Subjects :
- Cytoplasm
Programmed cell death
Molecular Sequence Data
Cell
Mutant
Active Transport, Cell Nucleus
Biophysics
Biology
Biochemistry
Cyclophilins
Cell Line, Tumor
Neoplasms
Two-Hybrid System Techniques
medicine
Humans
Amino Acid Sequence
Molecular Biology
Cellular localization
Cell Nucleus
Cell Biology
Cell biology
medicine.anatomical_structure
Apoptosis
Mutation
Cancer cell
Capsid Proteins
Nuclear localization sequence
Subjects
Details
- ISSN :
- 0006291X
- Volume :
- 372
- Database :
- OpenAIRE
- Journal :
- Biochemical and Biophysical Research Communications
- Accession number :
- edsair.doi.dedup.....f1940dee226b7f2c42d96ba345012fe7