Helmholtz Gemeinschaft


Periostin shows increased evolutionary plasticity in its alternatively spliced region

[thumbnail of 10721oa.pdf] PDF - Requires a PDF viewer such as GSview, Xpdf or Adobe Acrobat Reader

Item Type:Article
Title:Periostin shows increased evolutionary plasticity in its alternatively spliced region
Creators Name:Hoersch, S. and Andrade-Navarro, M.A.
Abstract:BACKGROUND: Periostin (POSTN) is a secreted extracellular matrix protein of poorly defined function that has been related to bone and heart development as well as to cancer. In human and mouse, it is known to undergo alternative splicing in its C-terminal region, which is devoid of known protein domains. Differential expression of periostin, sometimes of specific splicing isoforms, is observed in a broad range of human cancers, including breast, pancreatic, and colon cancer. Here, we combine genomic and transcriptomic sequence data from vertebrate organisms to study the evolution of periostin and particularly of its C-terminal region. RESULTS: We found that the C-terminal part of periostin is markedly more variable among vertebrates than the rest of periostin in terms of exon count, length, and splicing pattern, which we interpret as a consequence of neofunctionalization after the split between periostin and its paralog transforming growth factor, beta-induced (TGFBI). We also defined periostin's sequential 13-amino acid repeat units - well conserved in teleost fish, but more obscure in higher vertebrates - whose secondary structure is predicted to be consecutive beta strands. We suggest that these beta strands may mediate binding interactions with other proteins through an extended beta-zipper in a manner similar to the way repeat units in bacterial cell wall proteins have been reported to bind human fibronectin. CONCLUSIONS: Our results, obtained with the help of the increasingly large collection of complete vertebrate genomes, document the evolutionary plasticity of periostin's C-terminal region, and for the first time suggest a basis for its functional role.
Keywords:Alternative Splicing, Amino Acid Sequence, Cell Adhesion Molecules, Computational Biology, Molecular Evolution, Exons, Molecular Sequence Data, Phylogeny, Sequence Alignment, Vertebrates, Animals
Source:BMC Evolutionary Biology
Publisher:BioMed Central
Page Range:30
Date:28 January 2010
Official Publication:https://doi.org/10.1186/1471-2148-10-30
PubMed:View item in PubMed

Repository Staff Only: item control page


Downloads per month over past year

Open Access
MDC Library