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Vol. 12, Issue 4, 1061-1077, April 2001
-Actinin-like Protein in Fission
Yeast Cell Polarization and Cytokinesis
Department of Biology and Program in Molecular Biology and
Biotechnology, University of North Carolina, Chapel Hill, North
Carolina 27599
Eukaryotic cells contain many actin-interacting proteins, including
the 
-actinins and the fimbrins, both of which have actin cross-linking activity in vitro. We report here the identification and
characterization of both an -actinin-like protein (Ain1p) and a
fimbrin (Fim1p) in the fission yeast Schizosaccharomyces pombe. Ain1p localizes to the actomyosin-containing medial ring in an F-actin-dependent manner, and the Ain1p ring contracts during cytokinesis. ain1 deletion cells have no obvious defects
under normal growth conditions but display severe cytokinesis defects, associated with defects in medial-ring and septum formation, under certain stress conditions. Overexpression of Ain1p also causes cytokinesis defects, and the ain1 deletion shows
synthetic effects with other mutations known to affect medial-ring
positioning and/or organization. Fim1p localizes both to the cortical
actin patches and to the medial ring in an F-actin-dependent manner,
and several lines of evidence suggest that Fim1p is involved in
polarization of the actin cytoskeleton. Although a fim1
deletion strain has no detectable defect in cytokinesis, overexpression
of Fim1p causes a lethal cytokinesis defect associated with a failure
to form the medial ring and concentrate actin patches at the cell
middle. Moreover, an ain1 fim1 double mutant has a
synthetical-lethal defect in medial-ring assembly and cell division.
Thus, Ain1p and Fim1p appear to have an overlapping and essential
function in fission yeast cytokinesis. In addition,
protein-localization and mutant-phenotype data suggest that Fim1p, but
not Ain1p, plays important roles in mating and in spore formation.
Corresponding author. E-mail address:
jpringle{at}emailunc.edu.
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