Selectivity in subunit composition of Ena/VASP tetramers.

TitleSelectivity in subunit composition of Ena/VASP tetramers.
Publication TypeJournal Article
Year of Publication2015
AuthorsRiquelme, DN, Meyer, AS, Barzik, M, Keating, A, Gertler, FB
JournalBiosci Rep
Date Published2015

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.

Alternate JournalBiosci. Rep.
PubMed ID26221026
PubMed Central IDPMC4721544
Grant List1-DP5-OD019815 / OD / NIH HHS / United States
P30 CA014051 / CA / NCI NIH HHS / United States
P30-CA14051 / CA / NCI NIH HHS / United States
T32 GM007287 / GM / NIGMS NIH HHS / United States
T32GM007287 / GM / NIGMS NIH HHS / United States
U54-CA112967 / CA / NCI NIH HHS / United States