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Vol. 13, Issue 2, 469-479, February 2002
Department of Microbiology, University of Connecticut Health
Center, Farmington, Connecticut 06030-3205
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.
Present address: Plant Science Initiative,
University of Nebraska, N234 Beadle Center, Lincoln, NE
68588-0660.
Online version of this article contains video
material for some figures. Online version available at
www.molbiolcell.org.
*
Corresponding author. E-mail address:
sharri1{at}unlnotes.unl.edu.
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