Document Detail

Dynamics of the formin for3p in actin cable assembly.
MedLine Citation:
PMID:  16782006     Owner:  NLM     Status:  MEDLINE    
BACKGROUND: Formins are a conserved family of actin nucleators responsible for the assembly of diverse actin structures such as cytokinetic rings and filopodia. In the fission yeast Schizosaccharomyces pombe, the formin for3p is necessary for the formation of actin cables, which are bundles of short parallel actin filaments that regulate cell polarity. These filaments are largely organized with their barbed ends facing the cell tip, where for3p is thought to function in their assembly. RESULTS: Here, using a functional for3p-3GFP fusion expressed at endogenous levels, we find that for3p localizes to small dots that appear transiently at cell tips and then move away on actin cables at a rate of 0.3 microm/s. These movements were dependent on the continuous assembly of actin in cables, on the ability of for3p to bind actin within its FH2 domain, and on profilin and bud6p, two formin binding proteins that promote formin activity. Bud6p transiently colocalizes with for3p at the cell tip and stays behind at the cell tip when for3p detaches. CONCLUSIONS: These findings suggest a new model for actin cable assembly: a for3p particle is activated and promotes the assembly of a short actin filament at the cell tip for only seconds. For3p and the actin filament may then be released from the cell tip and carried passively into the cell interior by retrograde flow of actin filaments in the cable. These studies reveal a complex and dynamic cycle of formin regulation and actin cable assembly in vivo.
Sophie G Martin; Fred Chang
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Current biology : CB     Volume:  16     ISSN:  0960-9822     ISO Abbreviation:  Curr. Biol.     Publication Date:  2006 Jun 
Date Detail:
Created Date:  2006-06-19     Completed Date:  2006-08-23     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  9107782     Medline TA:  Curr Biol     Country:  England    
Other Details:
Languages:  eng     Pagination:  1161-70     Citation Subset:  IM    
Department of Microbiology, College of Physicians and Surgeons, Columbia University, 701 West 168th Street, New York, New York 10032, USA.
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MeSH Terms
Cell Cycle Proteins / analysis,  chemistry,  metabolism*
Fluorescence Recovery After Photobleaching
Green Fluorescent Proteins / analysis
Microfilaments / metabolism*
Microtubule-Associated Proteins / metabolism
Models, Biological
Profilins / metabolism
Protein Structure, Tertiary
Schizosaccharomyces / cytology,  metabolism*
Schizosaccharomyces pombe Proteins / analysis,  chemistry,  metabolism*
rho GTP-Binding Proteins / metabolism
Grant Support
Reg. No./Substance:
0/Cell Cycle Proteins; 0/FOR3 protein, S pombe; 0/Microtubule-Associated Proteins; 0/Profilins; 0/Schizosaccharomyces pombe Proteins; 0/Tea4 protein, S pombe; 0/cdc3 protein, S pombe; 0/rho3 protein, S pombe; 147336-22-9/Green Fluorescent Proteins; EC GTP-Binding Proteins
Comment In:
Curr Biol. 2006 Jul 25;16(14):R535-8   [PMID:  16860728 ]

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