Document Detail

Polarized actin bundles formed by human fascin-1: their sliding and disassembly on myosin II and myosin V in vitro.
MedLine Citation:
PMID:  14535950     Owner:  NLM     Status:  MEDLINE    
Fascin-1 is a putative bundling factor of actin filaments in the filopodia of neuronal growth cones. Here, we examined the structure of the actin bundle formed by human fascin-1 (actin/fascin bundle), and its mode of interaction with myosin in vitro. The distance between cross-linked filaments in the actin/bundle was 8-9 nm, and the bundle showed the transverse periodicity of 36 nm perpendicular to the bundle axis, which was confirmed by electron microscopy. Decoration of the actin/fascin bundle with heavy meromyosin revealed that the arrowheads of filaments in the bundle pointed in the same direction, indicating that the bundle has polarity. This result suggested that fascin-1 plays an essential role in polarity of actin bundles in filopodia. In the in vitro motility assay, actin/fascin bundles slid as fast as single actin filaments on myosin II and myosin V. When myosin was attached to the surface at high density, the actin/fascin bundle disassembled to single filaments at the pointed end of the bundle during sliding. These results suggest that myosins may drive filopodial actin bundles backward by interacting with actin filaments on the surface, and may induce disassembly of the bundle at the basal region of filopodia.
Ryoki Ishikawa; Takeshi Sakamoto; Toshio Ando; Sugie Higashi-Fujime; Kazuhiro Kohama
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of neurochemistry     Volume:  87     ISSN:  0022-3042     ISO Abbreviation:  J. Neurochem.     Publication Date:  2003 Nov 
Date Detail:
Created Date:  2003-10-10     Completed Date:  2003-11-24     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985190R     Medline TA:  J Neurochem     Country:  England    
Other Details:
Languages:  eng     Pagination:  676-85     Citation Subset:  IM    
Department of Pharmacology, Gunma University School of Medicine, Maebashi, Japan.
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MeSH Terms
Actins / chemistry*,  metabolism,  ultrastructure
Carrier Proteins / chemistry*,  metabolism,  ultrastructure
Growth Cones / physiology
Macromolecular Substances
Microfilament Proteins / chemistry*,  metabolism,  ultrastructure
Models, Biological
Muscle Contraction / physiology
Muscle, Skeletal / chemistry
Myosin Subfragments / chemistry
Myosin Type II / chemistry*,  metabolism
Myosin Type V / chemistry*,  metabolism
Pseudopodia / physiology
Reg. No./Substance:
0/Actins; 0/Carrier Proteins; 0/Macromolecular Substances; 0/Microfilament Proteins; 0/Myosin Subfragments; 146808-54-0/fascin; EC 3.6.1.-/Myosin Type II; EC 3.6.1.-/Myosin Type V

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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