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Vol. 12, Issue 11, 3515-3526, November 2001
*Division of Biology, Department of Life Sciences, Graduate Program
in Interdisciplinary Sciences, School of Arts and Sciences, University
of Tokyo, Komaba, Meguro-ku, Tokyo 153-8902, Japan;
We report studies of the fission yeast fimbrin-like protein Fim1,
which contains two EF-hand domains and two actin-binding domains (ABD1
and ABD2). Fim1 is a component of both F-actin patches and the F-actin
ring, but not of F-actin cables. Fim1 cross-links F-actin in
vitro, but a Fim1 protein lacking either EF-hand domains (Fim1A12) or both the EF-hand domains and ABD1 (Fim1A2) has no actin
cross-linking activity. Overexpression of Fim1 induced the formation of
F-actin patches throughout the cell cortex, whereas the F-actin patches
disappear in cells overexpressing Fim1A12 or Fim1A2. Thus, the actin
cross-linking activity of Fim1 is probably important for the formation
of F-actin patches. The overexpression of Fim1 also excluded the
actin-depolymerizing factor Adf1 from the F-actin patches and inhibited
the turnover of actin in these structures. Thus, Fim1 may function in
stabilizing the F-actin patches. We also isolated the gene encoding
Acp1, a subunit of the heterodimeric F-actin capping protein.
fim1 acp1 double null cells showed more severe defects
in the organization of the actin cytoskeleton than those seen in each
single mutant. Thus, Fim1 and Acp1 may function in a similar manner in
the organization of the actin cytoskeleton. Finally, genetic studies
suggested that Fim1 may function in cytokinesis in cooperation with
Cdc15 (PSTPIP) and Rng2 (IQGAP), respectively.
Graduate Program in Biophysics and Biochemistry, School
of Science, University of Tokyo, Hongo, Bunkyo-ku, Tokyo 113-0033, Japan; §Protein Biochemistry, Institute of Life Science,
Kurume University, Kurume 839-0861, Japan; and
Department of Cell Biology, National Institute for Basic
Biology, Okazaki 444-8585, Japan
Corresponding author. E-mail address:
cnakano{at}bio.c.u-tokyo.ac.jp.
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