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Vol. 14, Issue 7, 2617-2629, July 2003
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*Whitehead Institute for Biomedical Research and
Massachusetts Institute of Technology, Cambridge, Massachusetts 02142; and
Biology Department and Rosenstiel Center,
Brandeis University, Waltham, Massachusetts 02454
Submitted January 21, 2003;
Revised March 7, 2003;
Accepted March 7, 2003
Monitoring Editor: Anthony Bretscher
Calponins and transgelins are members of a conserved family of
actin-associated proteins widely expressed from yeast to humans. Although a
role for calponin in muscle cells has been described, the biochemical
activities and in vivo functions of nonmuscle calponins and transgelins are
largely unknown. Herein, we have used genetic and biochemical analyses to
characterize the budding yeast member of this family, Scp1, which most closely
resembles transgelin and contains one calponin homology (CH) domain. We show
that Scp1 is a novel component of yeast cortical actin patches and shares in
vivo functions and biochemical activities with Sac6/fimbrin, the one other
actin patch component that contains CH domains. Purified Scp1 binds directly
to filamentous actin, cross-links actin filaments, and stabilizes filaments
against disassembly. Sequences in Scp1 sufficient for actin binding and
cross-linking reside in its carboxy terminus, outside the CH domain.
Overexpression of SCP1 suppresses sac6
defects, and
deletion of SCP1 enhances sac6 defects. Together,
these data show that Scp1 and Sac6/fimbrin cooperate to stabilize and organize
the yeast actin cytoskeleton.
Abbreviations used: CH calponin homology, CLR calponin-like repeat. Supplementary video: Changes in GFP-Scp1 localization over time (consecutive frames taken at 3-s intervals).
Online version of this article contains video material for some figures.
Online version is available at
www.molbiolcell.org.
Corresponding author. E-mail address:
gfink{at}wi.mit.edu.
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