Selectivity in subunit composition of Ena/VASP tetramers
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Gertler_Selectivity in subunit.pdf
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Author(s) • • • •
Riquelme, Daisy Noelia
Meyer, Aaron Samuel
Barzik, Melanie
Keating, Amy E.
Gertler, Frank
Date Issued
July 2015
Journal
Bioscience Reports
Publisher
Portland Press
Citation
Riquelme, D. N. et al. “Selectivity in Subunit Composition of Ena/VASP Tetramers.” Bioscience Reports 35.5 (2015): e00246–e00246.
Version
Final published version
Abstract
The members of the actin regulatory family of Ena/VASP proteins form stable tetramers. The vertebrate members of the Ena/VASP family, VASP, Mena and EVL, have many overlapping properties and expression patterns, but functional and regulatory differences between paralogues have been observed. The formation of mixed oligomers may serve a regulatory role to refine Ena/VASP activity. While it has been assumed that family members can form mixed oligomers, this possibility has not been investigated systematically. Using cells expressing controlled combinations of VASP, Mena and EVL, we evaluated the composition of Ena/VASP oligomers and found that VASP forms oligomers without apparent bias with itself, Mena or EVL. However, Mena and EVL showed only weak hetero-oligomerization, suggesting specificity in the association of Ena/VASP family members. Co-expression of VASP increased the ability of Mena and EVL to form mixed oligomers. Additionally, we found that the tetramerization domain (TD) at the C-termini of Ena/VASP proteins conferred the observed selectivity. Finally, we demonstrate that replacement of the TD with a synthetic tetramerizing coiled coil sequence supports homo-oligomerization and normal VASP subcellular localization.
MIT Department
Massachusetts Institute of Technology. Department of Biological Engineering
Massachusetts Institute of Technology. Department of Biology
Koch Institute for Integrative Cancer Research at MIT
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Creative Commons Attribution 3.0 Unported licence
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DOI of Published Version
https://doi.org/10.1042/bsr20150149