Functional characterization and localization of the Aspergillus nidulans formin SEPA.
Formins are a family of multidomain scaffold proteins involved in actin-dependent morphogenetic events. In Aspergillus nidulans, the formin SEPA participates in two actin-mediated processes, septum formation and polarized growth. In this study, we use a new null mutant to demonstrate that SEPA is required for the formation of actin rings at septation sites. In addition, we find that a functional SEPA::GFP fusion protein localizes simultaneously to septation sites and hyphal tips, and that SEPA colocalizes with actin at each site. Using live imaging, we show that SEPA localization at septation sites and hyphal tips is dynamic. Notably, at septation sites, SEPA forms a ring that constricts as the septum is deposited. Moreover, we demonstrate that actin filaments are required to maintain the proper localization pattern of SEPA, and that the amino-terminal half of SEPA is sufficient for localization at septation sites and hyphal tips. In contrast, only localization at septation sites is affected by loss of the sepH gene product. We propose that specific morphological cues activate common molecular pathways to direct SEPA localization to the appropriate morphogenetic site.
Sharpless
Kathryn E
KE
Department of Microbiology, University of Connecticut Health Center, Farmington, Connecticut 06030-3205, USA.
Harris
Steven D
SD
D000199:Actins / Q000378:metabolism; D000595:Amino Acid Sequence; D001233:Aspergillus nidulans / Q000166:cytology / Q000235:genetics* / Q000378:metabolism; D016764:Cell Polarity; D005656:Fungal Proteins / Q000235:genetics* / Q000378:metabolism; D008969:Molecular Sequence Data; D009154:Mutation
D000199:Actins; D005656:Fungal Proteins; C093108:SEPA protein, Emericella nidulans