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

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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Fiedler T,Fabrice TN,Studer V,Vinet A,Faltova L,Kammerer RA,Steinmetz MO,Sharpe T,Pieters J

doi

10.1002/1873-3468.13787

subject

Has Abstract

pub_date

2020-04-16 00:00:00

eissn

0014-5793

issn

1873-3468

pub_type

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