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Different conformations of phosphatase and tensin homolog, deleted on chromosome 10 (PTEN) protein within the nucleus and cytoplasm of neurons.
- Source :
-
PloS one [PLoS One] 2011 Apr 29; Vol. 6 (4), pp. e18857. Date of Electronic Publication: 2011 Apr 29. - Publication Year :
- 2011
-
Abstract
- PTEN is a critical gene involved in the regulation of many cellular processes. The product of this gene has dual phosphatase activity and is able to dephosphorylate the 5' end of the phosphatidylinositol (3,4,5)-trisphosphate. Within the cellular nucleus, this protein has been associated with regulation of the expression of many genes, although the mechanism of this regulation remains unclear. In this paper, two specific oligonucleotide aptamers were developed and selected, using the SELEX procedure, according to their ability to detect the PTEN protein in different subcellular compartments of neurons. While one aptamer was able to detect PTEN in the nucleus, the other recognized PTEN in the cytoplasm. The recognition pattern of PTEN by both aptamers was confirmed using antibodies in western blots of the proteins purified from mouse cerebellar homogenates and subcellular fractions. Additionally, we demonstrated that the two aptamers recognized different epitopes of the target peptide. The results presented here could not be fully explained by the canonical phosphatase structure of PTEN, suggesting the existence of different conformations of phosphatase in the nucleus and the cytoplasm.
- Subjects :
- Amino Acid Motifs
Animals
Cell Membrane metabolism
Combinatorial Chemistry Techniques
Epitopes chemistry
Humans
Mice
Models, Biological
Oligonucleotides genetics
Peptides chemistry
Protein Conformation
Cell Nucleus metabolism
Cytoplasm metabolism
Neurons metabolism
PTEN Phosphohydrolase biosynthesis
Subjects
Details
- Language :
- English
- ISSN :
- 1932-6203
- Volume :
- 6
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- PloS one
- Publication Type :
- Academic Journal
- Accession number :
- 21559530
- Full Text :
- https://doi.org/10.1371/journal.pone.0018857