Self-Assembly of Filopodia-Like Structures on Supported Lipid Bilayers

Filopodia are finger-like protrusive structures, containing actin bundles. By incubating frog egg extracts with supported lipid bilayers containing phosphatidylinositol 4,5 bisphosphate, we have reconstituted the assembly of filopodia-like structures (FLSs). The actin assembles into parallel bundles...

Full description

Saved in:
Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 2010-09, Vol.329 (5997), p.1341-1345
Main Authors: Lee, Kwonmoo, Gallop, Jennifer L, Rambani, Komal, Kirschner, Marc W
Format: Article
Language:English
Subjects:
Actin Cytoskeleton - ultrastructure
Actin-Related Protein 2-3 Complex - metabolism
Actins
Actins - metabolism
Animals
Assembly
Biological and medical sciences
Bundles
Carrier Proteins - metabolism
Cell Adhesion Molecules - metabolism
Cell Membrane - metabolism
Elongation
Frogs
Fundamental and applied biological sciences. Psychology
Humans
Interactions. Associations
Intermolecular phenomena
Kinetics
Lipid Bilayers
Lipids
Membrane Microdomains
Membranes
Mice
Microfilament Proteins - metabolism
Microfilaments
Microscopy
Microtubule-Associated Proteins - metabolism
Molecular biophysics
Monomers
NADPH Dehydrogenase - metabolism
Nucleation
P branes
Phosphatidylinositol Phosphates - metabolism
Phosphoproteins - metabolism
Plasmids
Proteins
Pseudopodia
Pseudopodia - metabolism
Pseudopodia - ultrastructure
Recombinant Fusion Proteins - metabolism
Self assembly
Signal Transduction
Wiskott-Aldrich Syndrome Protein, Neuronal - metabolism
Xenopus
Xenopus Proteins - metabolism
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:Filopodia are finger-like protrusive structures, containing actin bundles. By incubating frog egg extracts with supported lipid bilayers containing phosphatidylinositol 4,5 bisphosphate, we have reconstituted the assembly of filopodia-like structures (FLSs). The actin assembles into parallel bundles, and known filopodial components localize to the tip and shaft. The filopodia tip complexes self-organize--they are not templated by preexisting membrane microdomains. The F-BAR domain protein toca-1 recruits N-WASP, followed by the Arp2/3 complex and actin. Elongation proteins, Diaphanous-related formin, VASP, and fascin are recruited subsequently. Although the Arp2/3 complex is required for FLS initiation, it is not essential for elongation, which involves formins. We propose that filopodia form via clustering of Arp2/3 complex activators, self-assembly of filopodial tip complexes on the membrane, and outgrowth of actin bundles.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.1191710