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. 2020 Apr 16.
doi: 10.1002/1873-3468.13787. Online ahead of print.

Homodimerization of coronin A through the C-terminal coiled-coil domain is essential for multicellular differentiation of Dictyostelium discoideum

Thomas Fiedler  1 , Tohnyui Ndinyanka Fabrice  1 , Vera Studer  1 , Adrien Vinet  1 , Lenka Faltova  2 , Richard A Kammerer  2 , Michel O Steinmetz  1   2 , Timothy Sharpe  1 , Jean Pieters  1
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Free article

Homodimerization of coronin A through the C-terminal coiled-coil domain is essential for multicellular differentiation of Dictyostelium discoideum

Thomas Fiedler et al. FEBS Lett. .
Free article

Abstract

Coronin proteins are widely expressed among eukaryotic organisms. Most coronins consist of a WD-repeat domain followed by a C-terminal coiled coil. Dictyostelium discoideum expresses a single short coronin coronin A, which has been implicated in both actin modulation and multicellular differentiation. Whether coronin A's coiled coil is important for functionality, as well as the oligomeric state of coronin A is not known. Here, we show that the coiled-coil domain in Dictyostelium coronin A functions in homodimerization, is dispensable for coronin A stability and localization but essential for multicellular differentiation. These results allow a better understanding of the role for the coiled-coil domain of coronin A in oligomerization and demonstrate that its presence is essential for multicellular differentiation.

Keywords: Dictyostelium discoideum; coiled coil; coronin A; multicellular differentiation.

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References

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