|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
5557
|
|
pubmed:dateCreated |
2002-2-8
|
|
pubmed:abstractText |
Lamellipodia are thin, veil-like extensions at the edge of cells that contain a dynamic array of actin filaments. We describe an approach for analyzing spatial regulation of actin polymerization and depolymerization in vivo in which we tracked single molecules of actin fused to the green fluorescent protein. Polymerization and the lifetime of actin filaments in lamellipodia were measured with high spatial precision. Basal polymerization and depolymerization occurred throughout lamellipodia with largely constant kinetics, and polymerization was promoted within one micron of the lamellipodium tip. Most of the actin filaments in the lamellipodium were generated by polymerization away from the tip.
|
|
pubmed:grant |
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Actin-Related Protein 2,
http://linkedlifedata.com/resource/pubmed/chemical/Actin-Related Protein 3,
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Biopolymers,
http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Depsipeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Green Fluorescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Luminescent Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides, Cyclic,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/jasplakinolide
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Feb
|
|
pubmed:issn |
1095-9203
|
|
pubmed:author |
|
|
pubmed:issnType |
Electronic
|
|
pubmed:day |
8
|
|
pubmed:volume |
295
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
1083-6
|
|
pubmed:dateRevised |
2011-11-17
|
|
pubmed:meshHeading |
pubmed-meshheading:11834838-Actin Cytoskeleton,
pubmed-meshheading:11834838-Actin-Related Protein 2,
pubmed-meshheading:11834838-Actin-Related Protein 3,
pubmed-meshheading:11834838-Actins,
pubmed-meshheading:11834838-Animals,
pubmed-meshheading:11834838-Biopolymers,
pubmed-meshheading:11834838-Cell Line,
pubmed-meshheading:11834838-Cytoskeletal Proteins,
pubmed-meshheading:11834838-Depsipeptides,
pubmed-meshheading:11834838-Fibroblasts,
pubmed-meshheading:11834838-Fluorescence,
pubmed-meshheading:11834838-Green Fluorescent Proteins,
pubmed-meshheading:11834838-Half-Life,
pubmed-meshheading:11834838-Luminescent Proteins,
pubmed-meshheading:11834838-Models, Biological,
pubmed-meshheading:11834838-Peptides, Cyclic,
pubmed-meshheading:11834838-Pseudopodia,
pubmed-meshheading:11834838-Recombinant Fusion Proteins,
pubmed-meshheading:11834838-Xenopus
|
|
pubmed:year |
2002
|
|
pubmed:articleTitle |
Single-molecule speckle analysis of actin filament turnover in lamellipodia.
|
|
pubmed:affiliation |
Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA. naoki_watanabe@hms.harvard.edu
|
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
|
