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 Lettjournal_title
FEBS lettersauthors
Fiedler T,Fabrice TN,Studer V,Vinet A,Faltova L,Kammerer RA,Steinmetz MO,Sharpe T,Pieters Jdoi
10.1002/1873-3468.13787subject
Has Abstractpub_date
2020-04-16 00:00:00eissn
0014-5793issn
1873-3468pub_type
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