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MBC in Press, published online ahead of print January 9, 2002
Mol. Biol. Cell 10.1091/mbc.01-07-0356

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Submitted on July 18, 2001
Revised on October 23, 2001
Accepted on November 5, 2001

Functional characterization and localization of the Aspergillus nidulans Formin SEPA

Kathryn E. Sharpless1 and Steven D. Harris2*

1 Department of Microbiology, University of Connecticut Health Center, 263 Farmington Avenue, Farmington, CT 06030-3205
2 Department of Microbiology, University of Connecticut Health Center, 263 Farmington Avenue, Farmington, CT 06030-3205 (Present address: Plant Science Initiative, University of Nebraska, N234 Beadle Center, Lincoln, NE 68588-0660)

* Corresponding author. E-mail address: sharri1{at}unlnotes.unl.edu.

Formins are a family of multi-domain 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 co-localizes 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.




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