Arp2/3 Is a Negative Regulator of Growth Cone Translocation

Arp2/3 is an actin binding complex that is enriched in the peripheral lamellipodia of fibroblasts, where it forms a network of short, branched actin filaments, generating the protrusive force that extends lamellipodia and drives fibroblast motility. Although it has been assumed that Arp2/3 would pla...

Full description

Saved in:
Bibliographic Details
Published in:Neuron (Cambridge, Mass.) Mass.), 2004-07, Vol.43 (1), p.81-94
Main Authors: Strasser, Geraldine A, Rahim, Nazimah Abdul, VanderWaal, Kristyn E, Gertler, Frank B, Lanier, Lorene M
Format: Article
Language:English
Subjects:
Actin Cytoskeleton - metabolism
Actin-Related Protein 2
Actin-Related Protein 3
Amino Acid Sequence - genetics
Animals
Animals, Newborn
Cell Differentiation - genetics
Cell Movement - genetics
Cells, Cultured
Cytoskeletal Proteins - genetics
Cytoskeletal Proteins - physiology
Cytoskeleton
Feedback, Physiological - genetics
Fetus
Green Fluorescent Proteins
Growth Cones - metabolism
Growth Cones - ultrastructure
Luminescent Proteins
Macromolecular Substances
Mice
Microtubules - metabolism
Motility
Nervous System - cytology
Nervous System - embryology
Nervous System - metabolism
Polymerization
Protein Binding - genetics
Protein Structure, Tertiary - genetics
Proteins
Pseudopodia - metabolism
Pseudopodia - ultrastructure
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Arp2/3 is an actin binding complex that is enriched in the peripheral lamellipodia of fibroblasts, where it forms a network of short, branched actin filaments, generating the protrusive force that extends lamellipodia and drives fibroblast motility. Although it has been assumed that Arp2/3 would play a similar role in growth cones, our studies indicate that Arp2/3 is enriched in the central, not the peripheral, region of growth cones and that the growth cone periphery contains few branched actin filaments. Arp2/3 inhibition in fibroblasts severely disrupts actin organization and membrane protrusion. In contrast, Arp2/3 inhibition in growth cones minimally affects actin organization and does not inhibit lamellipodia protrusion or de novo filopodia formation. Surprisingly, Arp2/3 inhibition significantly enhances axon elongation and causes defects in growth cone guidance. These results indicate that Arp2/3 is a negative regulator of growth cone translocation.
ISSN:0896-6273
1097-4199
DOI:10.1016/j.neuron.2004.05.015