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PMID: 1608453 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Novel form of growth cone motility involving site-directed actin filament assembly.

Nature ·Vol. 357 ·No. 6378 ·1992-06-11 ·Pages 515-8

Forscher P, Lin CH, Thompson C

Abstract

Regulation of cytoskeletal structure and motility by extracellular signals is essential for all directed forms of cell movement and underlies the developmental process of axonal guidance in neuronal growth cones. Interaction with polycationic microbeads can trigger morphogenic changes in neurons and muscle cells normally associated with formation of pre- and postsynaptic specializations. Furthermore, when various types of microscopic particles are applied to the lamellar surface of a neuronal growth cone or motile cell they often exhibit retrograde movement at rates of 1-6 microns min-1 (refs 3-6). There is strong evidence that this form of particle movement results from translocation of membrane proteins associated with cortical F-actin networks, not from bulk retrograde lipid flow and may be a mechanism behind processes such as cell locomotion, growth cone migration and capping of cell-surface antigens. Here we report a new form of motility stimulated by polycationic bead interactions with the growth-cone membrane surface. Bead binding rapidly induces intracellular actin filament assembly, coincident with a production of force sufficient to drive bead movements. These extracellular bead movements resemble intracellular movements of bacterial parasites known to redirect host cell F-actin assembly for propulsion. Our results suggest that site-directed actin filament assembly may be a widespread cellular mechanism for generating force at membrane-cytoskeletal interfaces.

MeSH Terms
Actins/physiology,ultrastructure Animals Aplysia Bacteria Cations Cell Membrane/physiology,ultrastructure Cell Movement/physiology Cytochalasin B/pharmacology Cytoskeleton/ultrastructure Listeria monocytogenes Microspheres Neurons/ultrastructure
Chemicals
Actins Cations Cytochalasin B
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Forscher P
Department of Biology, Yale University, New Haven, Connecticut 06511.
Lin C H
Thompson C
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1992-06-11
Pages
515-8
Language
English
Region
England
NLM ID
0410462
Subset
IM
Corrections
CommentIn
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