期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 110, 期 24, 页码 9752-9757出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1308257110
关键词
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资金
- National Institutes of Health Research [GM026338, GM074739]
- National Science Foundation Presidential Early Career Award for Scientists and Engineers
- Howard Hughes Medical Institute
- Korean Research Foundation Grant [KRF-2008-357-C00048]
- National Research Foundation of Korea [2008-357-C00048] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
Formins promote processive elongation of actin filaments for cytokinetic contractile rings and other cellular structures. In vivo, these structures are exposed to tension, but the effect of tension on these processes was unknown. Here we used single-molecule imaging to investigate the effects of tension on actin polymerization mediated by yeast formin Bni1p. Small forces on the filaments dramatically slowed formin-mediated polymerization in the absence of profilin, but resulted in faster polymerization in the presence of profilin. We propose that force shifts the conformational equilibrium of the end of a filament associated with formin homology 2 domains toward the closed state that precludes polymerization, but that profilin-actin associated with formin homology 1 domains reverses this effect. Thus, physical forces strongly influence actin assembly by formin Bni1p.
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