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GASP/WFIKKN proteins: evolutionary aspects of their functions
Olivier Monestier1, Caroline Brun, Olivier Cocquempot
1INRA, UMR1061 Unité de Génétique Moléculaire Animale, Limoges, France.
Plos One
|September 1, 2012
Summary
Growth and differentiation factor Associated Serum Protein (GASP) 1 and 2 regulate myostatin activity. GASP1 shows stronger conservation, suggesting a key role in myostatin interaction and proteolysis prevention.
Area of Science:
- Evolutionary biology
- Molecular biology
- Developmental biology
Background:
- Growth and differentiation factor Associated Serum Protein (GASP) 1 and 2 are involved in myostatin activity control.
- Deuterostome GASPs possess a modular structure with WAP, follistatin/kazal, IGc2, kunitz, and NTR domains.
Purpose of the Study:
- To investigate the evolutionary history and functional divergence of GASP1 and GASP2.
- To elucidate the structural evolution of GASP proteins and their interaction with myostatin.
Main Methods:
- Independent phylogenetic analyses of GASP protein modules.
- Comparative analysis of substitution rates across GASP domains.
- In situ hybridization in mouse and zebrafish embryos.
Main Results:
- Papilin identified as a sister sequence to GASP, with divergence from the last common ancestor of Bilateria.
- GASP genes diverged during early vertebrate genome duplication.
- GASP1's follistatin/kazal domain shows higher conservation in mammals than GASP2, indicating stronger myostatin interaction.
- Follistatin and kunitz domain conservation increased from Ciona to early vertebrates.
- Gasp1 expression observed in somites and limb buds of mouse and zebrafish embryos.
Conclusions:
- The follistatin/kazal domain of GASP1 likely mediates a stronger interaction with myostatin.
- The second kunitz domain may prevent myostatin proteolysis.
- GASP evolution involved domain acquisition and gene duplication, contributing to vertebrate development.
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