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Updated: Jun 16, 2026

Detection of Alternative Splicing During Epithelial-Mesenchymal Transition
Published on: October 9, 2014
Periostin shows increased evolutionary plasticity in its alternatively spliced region
Sebastian Hoersch1, Miguel A Andrade-Navarro
1Bioinformatics and Computing Core, Koch Institute for Integrative Cancer Research, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge, MA 02139, USA. hoersch@mit.edu
The C-terminal region of periostin (POSTN) shows significant evolutionary changes across vertebrates, suggesting neofunctionalization and providing insights into its protein interactions and cancer-related roles.
Area of Science:
- Evolutionary biology
- Molecular biology
- Genomics
Background:
- Periostin (POSTN) is an extracellular matrix protein implicated in development and cancer.
- Its C-terminal region undergoes alternative splicing and lacks known protein domains.
- Differential POSTN expression and splicing are observed in various human cancers.
Purpose of the Study:
- To investigate the evolutionary history of periostin, focusing on its C-terminal region.
- To understand the functional implications of variations in POSTN's C-terminus.
Main Methods:
- Comparative analysis of genomic and transcriptomic data from vertebrate organisms.
- Examination of exon count, length, and splicing patterns of POSTN.
Main Results:
- The C-terminal region of POSTN exhibits high variability in exon count, length, and splicing across vertebrates.
- Identified conserved 13-amino acid repeat units in teleost fish, predicted to form beta strands.
- These beta strands may facilitate protein-protein interactions via a beta-zipper mechanism.
Conclusions:
- The C-terminal region of POSTN demonstrates significant evolutionary plasticity.
- These findings suggest a basis for POSTN's functional roles, potentially linked to its interaction capabilities.
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