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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
15
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pubmed:dateCreated |
1989-9-12
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pubmed:abstractText |
We have encapsulated actin filaments in the presence and absence of various actin-binding proteins into lipid vesicles. These vesicles are approximately the same size as animal cells and can be characterized by the same optical microscopic and mechanical techniques used to study cells. We demonstrate that the initially spherical vesicles can be forced into asymmetric, irregular shapes by polymerization of the actin that they contain. Deformation of the vesicles requires that the actin filaments be on average at least approximately 0.5 micron long as shown by the effects of gelsolin, an actin filament-nucleating protein. Filamin, a filament-crosslinking protein, caused the surfaces of the vesicles to have a smoother appearance. Heterogeneous distribution of actin filaments within the vesicles is caused by interfilament interactions and modulated by gelsolin and filamin. The vesicles provide a model system to study control of cell shape and cytoskeletal organization, membrane-cytoskeleton interactions, and cytomechanics.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/2548187-2454930,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2548187-279292,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2548187-2844828,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2548187-2881354,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2548187-3013849,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2548187-3029140,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2548187-3277283,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2548187-3293593,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2548187-3360852,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2548187-3527055,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2548187-3593872,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2548187-3603036,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2548187-3709419,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2548187-3709420,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2548187-3775380,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2548187-3821871,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2548187-4254541,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2548187-6048247,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2548187-6893667,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2548187-6994593,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2548187-7103505,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2548187-7115692,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2548187-7209484,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2548187-721823,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2548187-7356657,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2548187-786399,
http://linkedlifedata.com/resource/pubmed/commentcorrection/2548187-963074
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Actins,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Contractile Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Gelsolin,
http://linkedlifedata.com/resource/pubmed/chemical/Liposomes,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Microfilament Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylcholines,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylethanolamines,
http://linkedlifedata.com/resource/pubmed/chemical/filamins
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
86
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5773-7
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:2548187-Actins,
pubmed-meshheading:2548187-Animals,
pubmed-meshheading:2548187-Calcium-Binding Proteins,
pubmed-meshheading:2548187-Carrier Proteins,
pubmed-meshheading:2548187-Contractile Proteins,
pubmed-meshheading:2548187-Gelsolin,
pubmed-meshheading:2548187-Liposomes,
pubmed-meshheading:2548187-Macromolecular Substances,
pubmed-meshheading:2548187-Microfilament Proteins,
pubmed-meshheading:2548187-Muscles,
pubmed-meshheading:2548187-Phosphatidylcholines,
pubmed-meshheading:2548187-Phosphatidylethanolamines,
pubmed-meshheading:2548187-Protein Binding,
pubmed-meshheading:2548187-Rabbits,
pubmed-meshheading:2548187-Spectrometry, Fluorescence
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pubmed:year |
1989
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pubmed:articleTitle |
Actin polymerization induces a shape change in actin-containing vesicles.
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pubmed:affiliation |
Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, Saint Louis, MO 63110.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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